| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0541 | MJ_0917 | MJ_0541 | MJ_0917 | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...] | 0.923 |
| MJ_0541 | nadA | MJ_0541 | MJ_0407 | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | Quinolinate synthetase (nadA); Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 0.673 |
| MJ_0541 | nadC | MJ_0541 | MJ_0493 | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | Nicotinate-nucleotide pyrophosphorylase (nadC); Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. | 0.970 |
| MJ_0541 | nadE | MJ_0541 | MJ_1352 | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.962 |
| MJ_0541 | nadX | MJ_0541 | MJ_0915 | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | Conserved hypothetical protein; Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. | 0.655 |
| MJ_0806 | mdh | MJ_0806 | MJ_0490 | X-pro aminopeptidase (pepQ); Similar to SP:P46545 PID:1150454 PID:609078 percent identity: 33.33; identified by sequence similarity; putative. | L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily. | 0.470 |
| MJ_0806 | nadE | MJ_0806 | MJ_1352 | X-pro aminopeptidase (pepQ); Similar to SP:P46545 PID:1150454 PID:609078 percent identity: 33.33; identified by sequence similarity; putative. | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.513 |
| MJ_0917 | MJ_0541 | MJ_0917 | MJ_0541 | Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...] | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | 0.923 |
| MJ_0917 | nadC | MJ_0917 | MJ_0493 | Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...] | Nicotinate-nucleotide pyrophosphorylase (nadC); Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. | 0.427 |
| MJ_0917 | nadE | MJ_0917 | MJ_1352 | Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...] | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.955 |
| MJ_0917 | nadX | MJ_0917 | MJ_0915 | Conserved hypothetical protein; Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the phys [...] | Conserved hypothetical protein; Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. | 0.454 |
| MJ_1399 | nadE | MJ_1399 | MJ_1352 | Alignment in; Identified by sequence similarity; putative; Belongs to the UPF0200 family. | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.549 |
| MJ_1521 | nadE | MJ_1521 | MJ_1352 | Na+/H+ antiporter; This is probably a Na(+)/H(+) antiporter; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.638 |
| glnA | mdh | MJ_1346 | MJ_0490 | Glutamine synthetase (glnA); Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate. | L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily. | 0.462 |
| glnA | nadA | MJ_1346 | MJ_0407 | Glutamine synthetase (glnA); Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate. | Quinolinate synthetase (nadA); Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | 0.523 |
| glnA | nadE | MJ_1346 | MJ_1352 | Glutamine synthetase (glnA); Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate. | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.628 |
| mdh | MJ_0806 | MJ_0490 | MJ_0806 | L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily. | X-pro aminopeptidase (pepQ); Similar to SP:P46545 PID:1150454 PID:609078 percent identity: 33.33; identified by sequence similarity; putative. | 0.470 |
| mdh | glnA | MJ_0490 | MJ_1346 | L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily. | Glutamine synthetase (glnA); Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Beta-glutamate is a much poorer substrate than alpha-glutamate. | 0.462 |
| mdh | nadE | MJ_0490 | MJ_1352 | L-lactate dehydrogenase EGAD|7256|705; Catalyzes the reversible oxidation of (S)-malate and (S)- sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate. Belongs to the LDH/MDH superfamily. | NH(3)-dependent NAD+ synthetase (nadE); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | 0.518 |
| nadA | MJ_0541 | MJ_0407 | MJ_0541 | Quinolinate synthetase (nadA); Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. | Conserved hypothetical protein; Similar to GP:1001812 percent identity: 32.62; identified by sequence similarity; putative; Belongs to the archaeal NMN adenylyltransferase family. | 0.673 |
