| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM1549 | STM1550 | STM1549 | STM1550 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74636.1); Blastp hit to AAC74636.1 (95 aa), 62% identity in aa 1 - 87. | 0.518 |
| STM1549 | STM1551 | STM1549 | STM1551 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putative cytoplasmic protein. | 0.482 |
| STM1549 | carB | STM1549 | STM0067 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Carbamoyl-phosphate synthase large chain. (SW:CARB_SALTY). | 0.500 |
| STM1549 | dpaL | STM1549 | STM1002 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | 0.673 |
| STM1549 | ilvA | STM1549 | STM3905 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Threonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity). Belongs to the serine/threon [...] | 0.410 |
| STM1549 | tdcB | STM1549 | STM3244 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. TdcB also dehydrates serine to yield pyruv [...] | 0.476 |
| STM1549 | yjeF | STM1549 | STM4356 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putative sugar kinase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both ep [...] | 0.463 |
| STM1549 | yjgF | STM1549 | STM4458 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putative translation initiation inhibitor; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities and to avoid they are captured by anthranilate phosphoribosyltransferase (TrpD) to generate PRA, an intermediate in the alternative pyrimidine biosynthetic (APB) pathwa [...] | 0.826 |
| STM1549 | yoaB | STM1549 | STM1822 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC74879.1); Blastp hit to AAC74879.1 (130 aa), 92% identity in aa 17 - 130. | 0.954 |
| STM1549 | yqjG | STM1549 | STM3233 | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | Putative glutathione S-transferase; Similar to E. coli putative transferase (AAC76137.1); Blastp hit to AAC76137.1 (328 aa), 92% identity in aa 1 - 328. | 0.408 |
| STM1550 | STM1549 | STM1550 | STM1549 | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74636.1); Blastp hit to AAC74636.1 (95 aa), 62% identity in aa 1 - 87. | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | 0.518 |
| STM1550 | STM1551 | STM1550 | STM1551 | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74636.1); Blastp hit to AAC74636.1 (95 aa), 62% identity in aa 1 - 87. | Putative cytoplasmic protein. | 0.973 |
| STM1551 | STM1549 | STM1551 | STM1549 | Putative cytoplasmic protein. | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | 0.482 |
| STM1551 | STM1550 | STM1551 | STM1550 | Putative cytoplasmic protein. | Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74636.1); Blastp hit to AAC74636.1 (95 aa), 62% identity in aa 1 - 87. | 0.973 |
| carB | STM1549 | STM0067 | STM1549 | Carbamoyl-phosphate synthase large chain. (SW:CARB_SALTY). | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | 0.500 |
| dpaL | STM1549 | STM1002 | STM1549 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC77205.1); Blastp hit to AAC77205.1 (131 aa), 82% identity in aa 1 - 129. | 0.673 |
| dpaL | ilvA | STM1002 | STM3905 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Threonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity). Belongs to the serine/threon [...] | 0.426 |
| dpaL | tdcB | STM1002 | STM3244 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. TdcB also dehydrates serine to yield pyruv [...] | 0.828 |
| dpaL | yjgF | STM1002 | STM4458 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Putative translation initiation inhibitor; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities and to avoid they are captured by anthranilate phosphoribosyltransferase (TrpD) to generate PRA, an intermediate in the alternative pyrimidine biosynthetic (APB) pathwa [...] | 0.922 |
| dpaL | yoaB | STM1002 | STM1822 | Putatiave diaminopropionate ammonia lyase; Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position. In vivo L-, D- and a mixure of DL-DAP allow growth. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. | Putative translation initiation inhibitor; Similar to E. coli orf, hypothetical protein (AAC74879.1); Blastp hit to AAC74879.1 (130 aa), 92% identity in aa 17 - 130. | 0.439 |