| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| gltA | gudB | BSU18450 | BSU22960 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | 0.993 |
| gltA | proG | BSU18450 | BSU12910 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.503 |
| gltA | proH | BSU18450 | BSU18480 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.564 |
| gltA | proI | BSU18450 | BSU23800 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.503 |
| gltA | proJ | BSU18450 | BSU18470 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | 0.574 |
| gltA | putC | BSU18450 | BSU03210 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | 1-pyrroline-5-carboxylate dehydrogenase; Important for the use of proline as a sole carbon and energy source or a sole nitrogen source. | 0.935 |
| gltA | rocD | BSU18450 | BSU40340 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Ornithine aminotransferase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism. | 0.563 |
| gltA | rocG | BSU18450 | BSU37790 | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...] | 0.996 |
| gudB | gltA | BSU22960 | BSU18450 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | 0.993 |
| gudB | proJ | BSU22960 | BSU18470 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | 0.563 |
| gudB | putB | BSU22960 | BSU03200 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | Proline oxidase; Converts proline to delta-1-pyrroline-5-carboxylate. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source. | 0.513 |
| gudB | putC | BSU22960 | BSU03210 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | 1-pyrroline-5-carboxylate dehydrogenase; Important for the use of proline as a sole carbon and energy source or a sole nitrogen source. | 0.924 |
| gudB | putM | BSU22960 | BSU32850 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | Proline dehydrogenase 1; Converts proline to delta-1-pyrroline-5-carboxylate. | 0.472 |
| gudB | rocD | BSU22960 | BSU40340 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | Ornithine aminotransferase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism. | 0.631 |
| gudB | rocG | BSU22960 | BSU37790 | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] | Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...] | 0.905 |
| proG | gltA | BSU12910 | BSU18450 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. | 0.503 |
| proG | proH | BSU12910 | BSU18480 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.949 |
| proG | proI | BSU12910 | BSU23800 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | 0.952 |
| proG | proJ | BSU12910 | BSU18470 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | Glutamate 5-kinase; Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | 0.863 |
| proG | putB | BSU12910 | BSU03200 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. | Proline oxidase; Converts proline to delta-1-pyrroline-5-carboxylate. Important for the use of proline as a sole carbon and energy source or a sole nitrogen source. | 0.932 |
