node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Tchl_1035 | Tchl_1036 | Tchl_1035 | Tchl_1036 | Putative metal-dependent hydrolase. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.699 |
Tchl_1036 | Tchl_1035 | Tchl_1036 | Tchl_1035 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Putative metal-dependent hydrolase. | 0.699 |
Tchl_1036 | Tchl_1170 | Tchl_1036 | Tchl_1170 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | MBL-fold metallo hydrolase family protein. | 0.907 |
Tchl_1036 | Tchl_1706 | Tchl_1036 | Tchl_1706 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Dioxygenase superfamily protein. | 0.900 |
Tchl_1036 | Tchl_2264 | Tchl_1036 | Tchl_2264 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
Tchl_1036 | gloB | Tchl_1036 | Tchl_2858 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.969 |
Tchl_1036 | icmF | Tchl_1036 | Tchl_1708 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Fused isobutyryl-CoA mutase; Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. | 0.552 |
Tchl_1036 | ilvA | Tchl_1036 | Tchl_1527 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.828 |
Tchl_1036 | trpA | Tchl_1036 | Tchl_3355 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. | 0.800 |
Tchl_1036 | trpB | Tchl_1036 | Tchl_0541 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Tryptophan synthase beta chain like; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.800 |
Tchl_1036 | trpB-2 | Tchl_1036 | Tchl_3356 | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. | 0.819 |
Tchl_1170 | Tchl_1036 | Tchl_1170 | Tchl_1036 | MBL-fold metallo hydrolase family protein. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.907 |
Tchl_1170 | Tchl_1706 | Tchl_1170 | Tchl_1706 | MBL-fold metallo hydrolase family protein. | Dioxygenase superfamily protein. | 0.901 |
Tchl_1170 | gloB | Tchl_1170 | Tchl_2858 | MBL-fold metallo hydrolase family protein. | Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.916 |
Tchl_1706 | Tchl_1036 | Tchl_1706 | Tchl_1036 | Dioxygenase superfamily protein. | Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. | 0.900 |
Tchl_1706 | Tchl_1170 | Tchl_1706 | Tchl_1170 | Dioxygenase superfamily protein. | MBL-fold metallo hydrolase family protein. | 0.901 |
Tchl_1706 | Tchl_2264 | Tchl_1706 | Tchl_2264 | Dioxygenase superfamily protein. | L-serine dehydratase; Belongs to the iron-sulfur dependent L-serine dehydratase family. | 0.800 |
Tchl_1706 | gloB | Tchl_1706 | Tchl_2858 | Dioxygenase superfamily protein. | Hydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. | 0.901 |
Tchl_1706 | icmF | Tchl_1706 | Tchl_1708 | Dioxygenase superfamily protein. | Fused isobutyryl-CoA mutase; Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly. | 0.693 |
Tchl_1706 | ilvA | Tchl_1706 | Tchl_1527 | Dioxygenase superfamily protein. | L-threonine dehydratase biosynthetic IlvA; 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. | 0.822 |