| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MJ_0226 | MJ_0936 | MJ_0226 | MJ_0936 | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than X [...] | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.775 |
| MJ_0736 | MJ_0936 | MJ_0736 | MJ_0936 | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.793 |
| MJ_0920 | MJ_0936 | MJ_0920 | MJ_0936 | GTP-binding protein homologue (yphC); Similar to PID:1146219 SP:P50743 GB:AL009126 percent identity: 26.99; identified by sequence similarity; putative. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.434 |
| MJ_0934 | MJ_0935 | MJ_0934 | MJ_0935 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.952 |
| MJ_0934 | MJ_0936 | MJ_0934 | MJ_0936 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.597 |
| MJ_0934 | purD | MJ_0934 | MJ_0937 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.432 |
| MJ_0935 | MJ_0934 | MJ_0935 | MJ_0934 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.952 |
| MJ_0935 | MJ_0936 | MJ_0935 | MJ_0936 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.816 |
| MJ_0935 | purD | MJ_0935 | MJ_0937 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.448 |
| MJ_0936 | MJ_0226 | MJ_0936 | MJ_0226 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house- cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than X [...] | 0.775 |
| MJ_0936 | MJ_0736 | MJ_0936 | MJ_0736 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Alkyl hydroperoxide reductase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | 0.793 |
| MJ_0936 | MJ_0920 | MJ_0936 | MJ_0920 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | GTP-binding protein homologue (yphC); Similar to PID:1146219 SP:P50743 GB:AL009126 percent identity: 26.99; identified by sequence similarity; putative. | 0.434 |
| MJ_0936 | MJ_0934 | MJ_0936 | MJ_0934 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.597 |
| MJ_0936 | MJ_0935 | MJ_0936 | MJ_0935 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.816 |
| MJ_0936 | purD | MJ_0936 | MJ_0937 | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | 0.898 |
| purD | MJ_0934 | MJ_0937 | MJ_0934 | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.432 |
| purD | MJ_0935 | MJ_0937 | MJ_0935 | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 31.97; identified by sequence similarity; putative. | 0.448 |
| purD | MJ_0936 | MJ_0937 | MJ_0936 | Phosphoribosylamine--glycine ligase (purD); Similar to GB:J02732 SP:P12039 PID:143374 GB:AL009126 percent identity: 33.73; identified by sequence similarity; putative. | Conserved hypothetical protein; Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown. | 0.898 |