| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM0458 | STM1549 | STM0458 | STM1549 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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. | 0.608 |
| STM0458 | dpaL | STM0458 | STM1002 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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. | 0.903 |
| STM0458 | tdcB | STM0458 | STM3244 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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 [...] | 0.499 |
| STM0458 | yjgF | STM0458 | STM4458 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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 [...] | 0.435 |
| STM0458 | yoaB | STM0458 | STM1822 | Putative cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 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. | 0.607 |
| STM1003 | dpaL | STM1003 | STM1002 | Putative transcriptional regulator, Lrp family; Similar to E. coli inner membrane transport protein (AAC73118.1); Blastp hit to AAC73118.1 (476 aa), 30% identity in aa 12 - 430. | 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. | 0.771 |
| STM1549 | STM0458 | STM1549 | STM0458 | 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 cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 0.608 |
| 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. | 0.714 |
| 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 [...] | 0.520 |
| 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 [...] | 0.821 |
| 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. | 0.952 |
| allC | dpaL | STM0527 | STM1002 | Allantoate amidohydrolase; Similar to E. coli putative hydantoin utilization protein (AAC73618.1); Blastp hit to AAC73618.1 (411 aa), 88% identity in aa 1 - 411. | 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. | 0.855 |
| argE | dpaL | STM4120 | STM1002 | Acetylornithine deacetylase; Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. | 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. | 0.920 |
| argE | ilvE | STM4120 | STM3903 | Acetylornithine deacetylase; Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.699 |
| dpaL | STM0458 | STM1002 | STM0458 | 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 cysteine synthase/cystathionine beta-synthase; Similar to E. coli cysteine synthase B, O-acetylserine sulfhydrolase B (AAC75474.1); Blastp hit to AAC75474.1 (303 aa), 26% identity in aa 6 - 207, 35% identity in aa 198 - 289. | 0.903 |
| dpaL | STM1003 | STM1002 | STM1003 | 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 transcriptional regulator, Lrp family; Similar to E. coli inner membrane transport protein (AAC73118.1); Blastp hit to AAC73118.1 (476 aa), 30% identity in aa 12 - 430. | 0.771 |
| 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. | 0.714 |
| dpaL | allC | STM1002 | STM0527 | 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. | Allantoate amidohydrolase; Similar to E. coli putative hydantoin utilization protein (AAC73618.1); Blastp hit to AAC73618.1 (411 aa), 88% identity in aa 1 - 411. | 0.855 |
| dpaL | argE | STM1002 | STM4120 | 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. | Acetylornithine deacetylase; Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. | 0.920 |
| dpaL | ilvE | STM1002 | STM3903 | 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. | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.823 |