node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
atpD | gyrB | b3732 | b3699 | F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] | 0.921 |
atpD | rpoA | b3732 | b3295 | F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. | 0.925 |
atpD | rpoB | b3732 | b3987 | F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.982 |
gyrB | atpD | b3699 | b3732 | DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] | F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.921 |
gyrB | rpoA | b3699 | b3295 | DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. | 0.755 |
gyrB | rpoB | b3699 | b3987 | DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] | RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.977 |
rpoA | atpD | b3295 | b3732 | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. | F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.925 |
rpoA | gyrB | b3295 | b3699 | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. | DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] | 0.755 |
rpoA | rpoB | b3295 | b3987 | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. | RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | 0.999 |
rpoB | atpD | b3987 | b3732 | RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | F1 sector of membrane-bound ATP synthase, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | 0.982 |
rpoB | gyrB | b3987 | b3699 | RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | DNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] | 0.977 |
rpoB | rpoA | b3987 | b3295 | RNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | RNA polymerase, alpha subunit; DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit plays an important role in subunit assembly since its dimerization is the first step in the sequential assembly of subunits to form the holoenzyme. | 0.999 |