| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKB11964.1 | AKB11965.1 | MSTHT_0206 | MSTHT_0207 | NADH-quinone oxidoreductase subunit C/D. | NADH-quinone oxidoreductase subunit C/D. | 0.999 |
| AKB11964.1 | AKB12496.1 | MSTHT_0206 | MSTHT_0738 | NADH-quinone oxidoreductase subunit C/D. | Hypothetical protein. | 0.494 |
| AKB11964.1 | glmS | MSTHT_0206 | MSTHT_2544 | NADH-quinone oxidoreductase subunit C/D. | Glucosamine--fructose-6-phosphate aminotransferase (isomerizing); Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | 0.407 |
| AKB11964.1 | moaC | MSTHT_0206 | MSTHT_2465 | NADH-quinone oxidoreductase subunit C/D. | Molybdenum cofactor biosynthesis enzyme; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family. | 0.569 |
| AKB11964.1 | nnrD | MSTHT_0206 | MSTHT_2467 | NADH-quinone oxidoreductase subunit C/D. | NAD(P)HX epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epime [...] | 0.414 |
| AKB11965.1 | AKB11964.1 | MSTHT_0207 | MSTHT_0206 | NADH-quinone oxidoreductase subunit C/D. | NADH-quinone oxidoreductase subunit C/D. | 0.999 |
| AKB11965.1 | AKB12496.1 | MSTHT_0207 | MSTHT_0738 | NADH-quinone oxidoreductase subunit C/D. | Hypothetical protein. | 0.494 |
| AKB11965.1 | glmS | MSTHT_0207 | MSTHT_2544 | NADH-quinone oxidoreductase subunit C/D. | Glucosamine--fructose-6-phosphate aminotransferase (isomerizing); Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | 0.479 |
| AKB11965.1 | moaC | MSTHT_0207 | MSTHT_2465 | NADH-quinone oxidoreductase subunit C/D. | Molybdenum cofactor biosynthesis enzyme; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family. | 0.569 |
| AKB11965.1 | nnrD | MSTHT_0207 | MSTHT_2467 | NADH-quinone oxidoreductase subunit C/D. | NAD(P)HX epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epime [...] | 0.414 |
| AKB12220.1 | nnrD | MSTHT_0462 | MSTHT_2467 | Metallo-beta-lactamase family protein. | NAD(P)HX epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epime [...] | 0.452 |
| AKB12496.1 | AKB11964.1 | MSTHT_0738 | MSTHT_0206 | Hypothetical protein. | NADH-quinone oxidoreductase subunit C/D. | 0.494 |
| AKB12496.1 | AKB11965.1 | MSTHT_0738 | MSTHT_0207 | Hypothetical protein. | NADH-quinone oxidoreductase subunit C/D. | 0.494 |
| AKB12496.1 | AKB14172.1 | MSTHT_0738 | MSTHT_2414 | Hypothetical protein. | YgjD/Kae1/Qri7 family, required for N6-threonylcarbamoyl adenosine t(6)A37 modification in tRNA; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belo [...] | 0.468 |
| AKB12496.1 | dtdA | MSTHT_0738 | MSTHT_0683 | Hypothetical protein. | D-tyrosyl-tRNA(Tyr) deacylase; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. | 0.792 |
| AKB12496.1 | glmS | MSTHT_0738 | MSTHT_2544 | Hypothetical protein. | Glucosamine--fructose-6-phosphate aminotransferase (isomerizing); Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | 0.707 |
| AKB12496.1 | nnrD | MSTHT_0738 | MSTHT_2467 | Hypothetical protein. | NAD(P)HX epimerase; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epime [...] | 0.570 |
| AKB12496.1 | valS | MSTHT_0738 | MSTHT_2529 | Hypothetical protein. | Valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily. | 0.545 |
| AKB14172.1 | AKB12496.1 | MSTHT_2414 | MSTHT_0738 | YgjD/Kae1/Qri7 family, required for N6-threonylcarbamoyl adenosine t(6)A37 modification in tRNA; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belo [...] | Hypothetical protein. | 0.468 |
| AKB14172.1 | dtdA | MSTHT_2414 | MSTHT_0683 | YgjD/Kae1/Qri7 family, required for N6-threonylcarbamoyl adenosine t(6)A37 modification in tRNA; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function. In the N-terminal section; belo [...] | D-tyrosyl-tRNA(Tyr) deacylase; D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. | 0.486 |
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