node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CBH21558.1 | CBH22523.1 | CLOST_1438 | CLOST_2406 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Putative peroxiredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.939 |
CBH21558.1 | CBH22693.1 | CLOST_1438 | CLOST_2578 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Cysteine desulfurase family protein. | 0.912 |
CBH21558.1 | ahpC | CLOST_1438 | CLOST_2030 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Alkyl hydroperoxide reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | 0.939 |
CBH21558.1 | grdA | CLOST_1438 | CLOST_1112 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Glycine reductase component A selenoprotein; In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination. | 0.590 |
CBH21558.1 | megL | CLOST_1438 | CLOST_2039 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Methionine gamma-lyase. | 0.933 |
CBH21558.1 | selD | CLOST_1438 | CLOST_1359 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP. | 0.935 |
CBH21558.1 | trxA | CLOST_1438 | CLOST_1109 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Thioredoxin (Trx); Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.873 |
CBH21558.1 | trxB | CLOST_1438 | CLOST_1108 | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | Thioredoxin reductase. | 0.974 |
CBH22523.1 | CBH21558.1 | CLOST_2406 | CLOST_1438 | Putative peroxiredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 0.939 |
CBH22523.1 | trxA | CLOST_2406 | CLOST_1109 | Putative peroxiredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Thioredoxin (Trx); Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.479 |
CBH22523.1 | trxB | CLOST_2406 | CLOST_1108 | Putative peroxiredoxin; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | Thioredoxin reductase. | 0.732 |
CBH22693.1 | CBH21558.1 | CLOST_2578 | CLOST_1438 | Cysteine desulfurase family protein. | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 0.912 |
CBH22693.1 | selD | CLOST_2578 | CLOST_1359 | Cysteine desulfurase family protein. | Selenophosphate synthase; Synthesizes selenophosphate from selenide and ATP. | 0.938 |
CBH22693.1 | trxB | CLOST_2578 | CLOST_1108 | Cysteine desulfurase family protein. | Thioredoxin reductase. | 0.908 |
ahpC | CBH21558.1 | CLOST_2030 | CLOST_1438 | Alkyl hydroperoxide reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 0.939 |
ahpC | trxA | CLOST_2030 | CLOST_1109 | Alkyl hydroperoxide reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Thioredoxin (Trx); Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | 0.479 |
ahpC | trxB | CLOST_2030 | CLOST_1108 | Alkyl hydroperoxide reductase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. | Thioredoxin reductase. | 0.732 |
grdA | CBH21558.1 | CLOST_1112 | CLOST_1438 | Glycine reductase component A selenoprotein; In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination. | FAD-dependent pyridine nucleotide-disulphide oxidoreductase. | 0.590 |
grdA | grdE | CLOST_1112 | CLOST_1110 | Glycine reductase component A selenoprotein; In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination. | Glycine reductase complex component B subunits alpha and beta; In the first step of glycine reductase, the substrate is bound to component PB via a Schiff base intermediate. Then the PB- activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination (By similarity). | 0.945 |
grdA | grdX | CLOST_1112 | CLOST_1107 | Glycine reductase component A selenoprotein; In the first step of glycine, betaine and sarcosine reductases, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination. | GrdX protein; Function of strongly homologous gene; putative regulator. | 0.894 |