node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EIG53071.1 | EIG53215.1 | DesU5LDRAFT_1379 | DesU5LDRAFT_1531 | Glycine cleavage system T protein; PFAM: Aminomethyltransferase folate-binding domain; Glycine cleavage T-protein C-terminal barrel domain. | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | 0.913 |
EIG53071.1 | EIG54330.1 | DesU5LDRAFT_1379 | DesU5LDRAFT_2675 | Glycine cleavage system T protein; PFAM: Aminomethyltransferase folate-binding domain; Glycine cleavage T-protein C-terminal barrel domain. | PFAM: Methylenetetrahydrofolate reductase; TIGRFAM: 5,10-methylenetetrahydrofolate reductase, prokaryotic form; Belongs to the methylenetetrahydrofolate reductase family. | 0.879 |
EIG53071.1 | EIG54382.1 | DesU5LDRAFT_1379 | DesU5LDRAFT_2737 | Glycine cleavage system T protein; PFAM: Aminomethyltransferase folate-binding domain; Glycine cleavage T-protein C-terminal barrel domain. | Threonine dehydratase, medium form; 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. | 0.717 |
EIG53188.1 | EIG53215.1 | DesU5LDRAFT_1504 | DesU5LDRAFT_1531 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | 0.956 |
EIG53188.1 | EIG53344.1 | DesU5LDRAFT_1504 | DesU5LDRAFT_1664 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | Aspartate kinase, monofunctional class; PFAM: ACT domain; Amino acid kinase family; Belongs to the aspartokinase family. | 0.987 |
EIG53188.1 | EIG54330.1 | DesU5LDRAFT_1504 | DesU5LDRAFT_2675 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | PFAM: Methylenetetrahydrofolate reductase; TIGRFAM: 5,10-methylenetetrahydrofolate reductase, prokaryotic form; Belongs to the methylenetetrahydrofolate reductase family. | 0.901 |
EIG53188.1 | EIG54382.1 | DesU5LDRAFT_1504 | DesU5LDRAFT_2737 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | Threonine dehydratase, medium form; 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. | 0.930 |
EIG53188.1 | EIG55626.1 | DesU5LDRAFT_1504 | DesU5LDRAFT_4027 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.831 |
EIG53188.1 | EIG55627.1 | DesU5LDRAFT_1504 | DesU5LDRAFT_4028 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.825 |
EIG53188.1 | metXA | DesU5LDRAFT_1504 | DesU5LDRAFT_3208 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.845 |
EIG53188.1 | mtnA | DesU5LDRAFT_1504 | DesU5LDRAFT_2447 | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | S-methyl-5-thioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). | 0.458 |
EIG53215.1 | EIG53071.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_1379 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Glycine cleavage system T protein; PFAM: Aminomethyltransferase folate-binding domain; Glycine cleavage T-protein C-terminal barrel domain. | 0.913 |
EIG53215.1 | EIG53188.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_1504 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. | 0.956 |
EIG53215.1 | EIG53344.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_1664 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Aspartate kinase, monofunctional class; PFAM: ACT domain; Amino acid kinase family; Belongs to the aspartokinase family. | 0.913 |
EIG53215.1 | EIG53862.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_2196 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Hypothetical protein. | 0.972 |
EIG53215.1 | EIG54330.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_2675 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | PFAM: Methylenetetrahydrofolate reductase; TIGRFAM: 5,10-methylenetetrahydrofolate reductase, prokaryotic form; Belongs to the methylenetetrahydrofolate reductase family. | 0.997 |
EIG53215.1 | EIG54382.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_2737 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Threonine dehydratase, medium form; 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. | 0.916 |
EIG53215.1 | EIG55626.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_4027 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.967 |
EIG53215.1 | EIG55627.1 | DesU5LDRAFT_1531 | DesU5LDRAFT_4028 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Cystathionine beta-lyase/cystathionine gamma-synthase; PFAM: Cys/Met metabolism PLP-dependent enzyme. | 0.967 |
EIG53215.1 | metXA | DesU5LDRAFT_1531 | DesU5LDRAFT_3208 | PFAM: Pterin binding enzyme; B12 binding domain; Homocysteine S-methyltransferase. | Homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | 0.955 |