node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ABX20362.1 | eutC | SARI_00426 | SARI_00427 | Hypothetical protein; KEGG: spt:SPA0410 1.3e-241 eutB; ethanolamine ammonia-lyase heavy chain K03735; COG: COG4303 Ethanolamine ammonia-lyase, large subunit. | Hypothetical protein; KEGG: stm:STM2457 1.2e-149 eutC; ethanolamine ammonia-lyase, light chain K03736; COG: COG4302 Ethanolamine ammonia-lyase, small subunit; Psort location: Cytoplasmic, score:8.96; Belongs to the EutC family. | 0.999 |
ABX20618.1 | ABX21019.1 | SARI_00695 | SARI_01113 | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.905 |
ABX20618.1 | ABX24153.1 | SARI_00695 | SARI_04375 | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; 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. | 0.911 |
ABX20618.1 | ABX24157.1 | SARI_00695 | SARI_04379 | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: spt:SPA3109 1.4e-230 tdcG; L-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.905 |
ABX20618.1 | ABX24456.1 | SARI_00695 | SARI_04692 | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: stm:STM2971 9.4e-239 sdaB; L-serine dehydratase (L-threonine deaminase 2) K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.906 |
ABX20618.1 | dsdA | SARI_00695 | SARI_03847 | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: sec:SC3724 6.0e-228 dsdA; D-serine deaminase (dehydratase) K01753; COG: COG3048 D-serine dehydratase; Psort location: Cytoplasmic, score:8.96. | 0.907 |
ABX20618.1 | ilvA | SARI_00695 | SARI_03747 | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; 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. | 0.911 |
ABX21019.1 | ABX20618.1 | SARI_01113 | SARI_00695 | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.905 |
ABX21019.1 | ABX24153.1 | SARI_01113 | SARI_04375 | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; 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. | 0.911 |
ABX21019.1 | ABX24157.1 | SARI_01113 | SARI_04379 | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: spt:SPA3109 1.4e-230 tdcG; L-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.901 |
ABX21019.1 | ABX24456.1 | SARI_01113 | SARI_04692 | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: stm:STM2971 9.4e-239 sdaB; L-serine dehydratase (L-threonine deaminase 2) K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.903 |
ABX21019.1 | dsdA | SARI_01113 | SARI_03847 | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: sec:SC3724 6.0e-228 dsdA; D-serine deaminase (dehydratase) K01753; COG: COG3048 D-serine dehydratase; Psort location: Cytoplasmic, score:8.96. | 0.907 |
ABX21019.1 | ilvA | SARI_01113 | SARI_03747 | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; 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. | 0.912 |
ABX24153.1 | ABX20618.1 | SARI_04375 | SARI_00695 | Hypothetical protein; 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. | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.911 |
ABX24153.1 | ABX21019.1 | SARI_04375 | SARI_01113 | Hypothetical protein; 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. | Hypothetical protein; KEGG: stt:t1051 3.0e-242 sdaA; L-serine deaminase 1 K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.911 |
ABX24153.1 | ABX24157.1 | SARI_04375 | SARI_04379 | Hypothetical protein; 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. | Hypothetical protein; KEGG: spt:SPA3109 1.4e-230 tdcG; L-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.943 |
ABX24153.1 | ABX24456.1 | SARI_04375 | SARI_04692 | Hypothetical protein; 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. | Hypothetical protein; KEGG: stm:STM2971 9.4e-239 sdaB; L-serine dehydratase (L-threonine deaminase 2) K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.911 |
ABX24153.1 | dsdA | SARI_04375 | SARI_03847 | Hypothetical protein; 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. | Hypothetical protein; KEGG: sec:SC3724 6.0e-228 dsdA; D-serine deaminase (dehydratase) K01753; COG: COG3048 D-serine dehydratase; Psort location: Cytoplasmic, score:8.96. | 0.907 |
ABX24153.1 | ilvA | SARI_04375 | SARI_03747 | Hypothetical protein; 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. | Hypothetical protein; 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. | 0.944 |
ABX24157.1 | ABX20618.1 | SARI_04379 | SARI_00695 | Hypothetical protein; KEGG: spt:SPA3109 1.4e-230 tdcG; L-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | Hypothetical protein; KEGG: sec:SC2212 1.3e-227 sdhL; putative D-serine dehydratase K01752; COG: COG1760 L-serine deaminase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.905 |