node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dat | gltA | BSU09670 | BSU18450 | D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essen [...] | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | 0.594 |
dat | putC | BSU09670 | BSU03210 | D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essen [...] | 1-pyrroline-5-carboxylate dehydrogenase; Important for the use of proline as a sole carbon and energy source or a sole nitrogen source | 0.926 |
gltA | dat | BSU18450 | BSU09670 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | D-alanine aminotransferase; Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second half-reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essen [...] | 0.594 |
gltA | gudB | BSU18450 | BSU22960 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | Cryptic catabolic nad-specific glutamate dehydrogenase gudb; 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 [...] | 0.996 |
gltA | proG | BSU18450 | BSU12910 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | 0.625 |
gltA | proH | BSU18450 | BSU18480 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | Pyrroline-5-carboxylate reductase 1; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | 0.694 |
gltA | proI | BSU18450 | BSU23800 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | Pyrroline-5-carboxylate reductase 2; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | 0.647 |
gltA | putC | BSU18450 | BSU03210 | Glutamate synthase (nadph) large chain; 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 | 0.938 |
gltA | rocD | BSU18450 | BSU40340 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | Ornithine--oxo-acid transaminase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism | 0.533 |
gltA | rocG | BSU18450 | BSU37790 | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | Catabolic nad-specific glutamate dehydrogenase rocg; 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 c [...] | 0.998 |
gudB | gltA | BSU22960 | BSU18450 | Cryptic catabolic nad-specific glutamate dehydrogenase gudb; 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 synthase (nadph) large chain; Belongs to the glutamate synthase family | 0.996 |
gudB | putC | BSU22960 | BSU03210 | Cryptic catabolic nad-specific glutamate dehydrogenase gudb; 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 [...] | 1-pyrroline-5-carboxylate dehydrogenase; Important for the use of proline as a sole carbon and energy source or a sole nitrogen source | 0.944 |
gudB | rocD | BSU22960 | BSU40340 | Cryptic catabolic nad-specific glutamate dehydrogenase gudb; 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 [...] | Ornithine--oxo-acid transaminase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism | 0.721 |
gudB | rocG | BSU22960 | BSU37790 | Cryptic catabolic nad-specific glutamate dehydrogenase gudb; 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 [...] | Catabolic nad-specific glutamate dehydrogenase rocg; 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 c [...] | 0.805 |
proG | gltA | BSU12910 | BSU18450 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | Glutamate synthase (nadph) large chain; Belongs to the glutamate synthase family | 0.625 |
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 1; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | 0.887 |
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 2; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | 0.896 |
proG | putB | BSU12910 | BSU03200 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | Proline dehydrogenase 2; 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 | 0.880 |
proG | putC | BSU12910 | BSU03210 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | 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 |
proG | putM | BSU12910 | BSU32850 | Redundant pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline | Proline dehydrogenase 1; Converts proline to delta-1-pyrroline-5-carboxylate | 0.843 |