| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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. | 0.770 |
| 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 | 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 | 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 |
| 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. | 0.852 |
| alr | dpaL | STM4247 | STM1002 | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | 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. | 0.783 |
| alr | gltB | STM4247 | STM3330 | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | Similar to E. coli glutamate synthase, large subunit (AAC76244.1); Blastp hit to AAC76244.1 (1517 aa), 95% identity in aa 32 - 1517. | 0.813 |
| alr | glyA | STM4247 | STM2555 | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity). | 0.848 |
| alr | ilvE | STM4247 | STM3903 | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | Branched-chain amino-acid aminotransferase; Acts on leucine, isoleucine and valine. | 0.869 |
| alr | tdcB | STM4247 | STM3244 | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | 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 [...] | 0.487 |
| alr | yjgF | STM4247 | STM4458 | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | 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 [...] | 0.509 |
| 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. | 0.918 |
| 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. | 0.814 |
| 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. | 0.770 |
| 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 | 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. | 0.852 |
| dpaL | alr | STM1002 | STM4247 | 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. | Biosynthetic alanine racemase 1; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. | 0.783 |
| 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. | 0.918 |
| dpaL | gltB | STM1002 | STM3330 | 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. | Similar to E. coli glutamate synthase, large subunit (AAC76244.1); Blastp hit to AAC76244.1 (1517 aa), 95% identity in aa 32 - 1517. | 0.690 |
| dpaL | glyA | STM1002 | STM2555 | 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. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity). | 0.829 |
