node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ahpC | dsbC | b0605 | b2893 | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.526 |
ahpC | grxA | b0605 | b0849 | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | 0.734 |
ahpC | trxA | b0605 | b3781 | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.800 |
ahpC | trxB | b0605 | b0888 | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.990 |
ahpC | trxC | b0605 | b2582 | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Thioredoxin 2; Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin. | 0.767 |
ahpC | ygfK | b0605 | b2878 | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Putative Fe-S subunit oxidoreductase subunit; Could be an iron-sulfur flavoprotein with NADPH:O(2) oxidoreductase activity. | 0.409 |
dsbC | ahpC | b2893 | b0605 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.526 |
dsbC | grxA | b2893 | b0849 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | 0.414 |
dsbC | trxA | b2893 | b3781 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.828 |
dsbC | trxB | b2893 | b0888 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.922 |
dsbC | trxC | b2893 | b2582 | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | Thioredoxin 2; Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin. | 0.466 |
grxA | ahpC | b0849 | b0605 | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | Alkyl hydroperoxide reductase, C22 subunit; 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. Is the primary scavenger for endogenously generated hydrogen peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.734 |
grxA | dsbC | b0849 | b2893 | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | Protein disulfide isomerase II; Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. | 0.414 |
grxA | trxA | b0849 | b3781 | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | Thioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.779 |
grxA | trxB | b0849 | b0888 | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.914 |
grxA | trxC | b0849 | b2582 | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. | Thioredoxin 2; Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin. | 0.925 |
selD | sufS | b1764 | b1680 | Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP; Belongs to the selenophosphate synthase 1 family. Class I subfamily. | Cysteine desulfurase, stimulated by SufE; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd [...] | 0.965 |
selD | trxB | b1764 | b0888 | Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP; Belongs to the selenophosphate synthase 1 family. Class I subfamily. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.948 |
sufS | selD | b1680 | b1764 | Cysteine desulfurase, stimulated by SufE; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd [...] | Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP; Belongs to the selenophosphate synthase 1 family. Class I subfamily. | 0.965 |
sufS | trxB | b1680 | b0888 | Cysteine desulfurase, stimulated by SufE; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd [...] | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.945 |