| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Sfri_0426 | Sfri_2801 | Sfri_0426 | Sfri_2801 | PFAM: aminotransferase, class V; KEGG: son:SO4343 aminotransferase, class V. | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | 0.931 |
| Sfri_0426 | gcvP | Sfri_0426 | Sfri_3149 | PFAM: aminotransferase, class V; KEGG: son:SO4343 aminotransferase, class V. | Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.938 |
| Sfri_0426 | glyA | Sfri_0426 | Sfri_1033 | PFAM: aminotransferase, class V; KEGG: son:SO4343 aminotransferase, class V. | 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. | 0.942 |
| Sfri_0426 | ilvA | Sfri_0426 | Sfri_0425 | PFAM: aminotransferase, class V; KEGG: son:SO4343 aminotransferase, class V. | L-threonine ammonia-lyase; 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. | 0.926 |
| Sfri_0426 | kbl | Sfri_0426 | Sfri_3938 | PFAM: aminotransferase, class V; KEGG: son:SO4343 aminotransferase, class V. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.911 |
| Sfri_1898 | Sfri_2801 | Sfri_1898 | Sfri_2801 | PFAM: iron-containing alcohol dehydrogenase; aldehyde dehydrogenase; KEGG: son:SO2136 aldehyde-alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | 0.580 |
| Sfri_1898 | gcvP | Sfri_1898 | Sfri_3149 | PFAM: iron-containing alcohol dehydrogenase; aldehyde dehydrogenase; KEGG: son:SO2136 aldehyde-alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.543 |
| Sfri_1898 | ilvA | Sfri_1898 | Sfri_0425 | PFAM: iron-containing alcohol dehydrogenase; aldehyde dehydrogenase; KEGG: son:SO2136 aldehyde-alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | L-threonine ammonia-lyase; 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. | 0.452 |
| Sfri_1898 | tdh | Sfri_1898 | Sfri_3939 | PFAM: iron-containing alcohol dehydrogenase; aldehyde dehydrogenase; KEGG: son:SO2136 aldehyde-alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.552 |
| Sfri_2801 | Sfri_0426 | Sfri_2801 | Sfri_0426 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | PFAM: aminotransferase, class V; KEGG: son:SO4343 aminotransferase, class V. | 0.931 |
| Sfri_2801 | Sfri_1898 | Sfri_2801 | Sfri_1898 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | PFAM: iron-containing alcohol dehydrogenase; aldehyde dehydrogenase; KEGG: son:SO2136 aldehyde-alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. | 0.580 |
| Sfri_2801 | Sfri_2802 | Sfri_2801 | Sfri_2802 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | Thiol peroxidase (atypical 2-Cys peroxiredoxin); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | 0.628 |
| Sfri_2801 | Sfri_2904 | Sfri_2801 | Sfri_2904 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | KEGG: son:SO3413 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. | 0.927 |
| Sfri_2801 | gcvP | Sfri_2801 | Sfri_3149 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | Glycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.948 |
| Sfri_2801 | glyA | Sfri_2801 | Sfri_1033 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | 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. | 0.941 |
| Sfri_2801 | ilvA | Sfri_2801 | Sfri_0425 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | L-threonine ammonia-lyase; 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. | 0.935 |
| Sfri_2801 | kbl | Sfri_2801 | Sfri_3938 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | 2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. | 0.911 |
| Sfri_2801 | tdh | Sfri_2801 | Sfri_3939 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. | 0.902 |
| Sfri_2801 | ychF | Sfri_2801 | Sfri_0717 | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | GTP-binding protein YchF; ATPase that binds to both the 70S ribosome and the 50S ribosomal subunit in a nucleotide-independent manner. | 0.707 |
| Sfri_2802 | Sfri_2801 | Sfri_2802 | Sfri_2801 | Thiol peroxidase (atypical 2-Cys peroxiredoxin); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; KEGG: son:SO3338 L-allo-threonine aldolase. | 0.628 |