| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| glcD | glcF | BSU28680 | BSU28690 | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. | 0.999 |
| glcD | sspI | BSU28680 | BSU28660 | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | 0.401 |
| glcD | ysfB | BSU28680 | BSU28670 | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.694 |
| glcF | glcD | BSU28690 | BSU28680 | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. | 0.999 |
| glcF | sspI | BSU28690 | BSU28660 | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | 0.401 |
| glcF | ysfB | BSU28690 | BSU28670 | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.695 |
| glxK | ysfB | BSU40040 | BSU28670 | Glycerate kinase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.400 |
| pucR | ysfB | BSU32420 | BSU28670 | Transcriptional regulator of the purine degradation operon; Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression. Belongs to the CdaR family. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.535 |
| pucR | yukF | BSU32420 | BSU31920 | Transcriptional regulator of the purine degradation operon; Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression. Belongs to the CdaR family. | Putative transcriptional regulator; Mediates ald expression in response to alanine availability and is important for normal sporulation in B.subtilis. Belongs to the CdaR family. | 0.462 |
| putR | ysfB | BSU03230 | BSU28670 | Transcriptional activator of proline degradation operon; Activates transcription of the putBCP operon. Requires proline as a coactivator. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.500 |
| slpH | ysfB | BSU10940 | BSU28670 | 2-phosphosulfolactate phosphatase; Evidence 2b: Function of strongly homologous gene; enzyme; Belongs to the ComB family. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.463 |
| sspI | glcD | BSU28660 | BSU28680 | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. | 0.401 |
| sspI | glcF | BSU28660 | BSU28690 | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. | 0.401 |
| sspI | ysfB | BSU28660 | BSU28670 | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | 0.577 |
| sspI | ysgA | BSU28660 | BSU28650 | Small acid-soluble spore protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the SspI family. | Putative RNA methylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. | 0.600 |
| ysfB | glcD | BSU28670 | BSU28680 | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. | 0.694 |
| ysfB | glcF | BSU28670 | BSU28690 | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | Glycolate oxidase iron-sulfur subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. | 0.695 |
| ysfB | glxK | BSU28670 | BSU40040 | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | Glycerate kinase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. | 0.400 |
| ysfB | pucR | BSU28670 | BSU32420 | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | Transcriptional regulator of the purine degradation operon; Activates the expression of pucFG, pucH, pucI, pucJKLM and guaD, while it represses pucABCDE and its own expression. Belongs to the CdaR family. | 0.535 |
| ysfB | putR | BSU28670 | BSU03230 | Putative regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the CdaR family. | Transcriptional activator of proline degradation operon; Activates transcription of the putBCP operon. Requires proline as a coactivator. | 0.500 |