node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
MJ_0514.2 | MJ_0934 | MJ_0514.2 | MJ_0934 | Polyferredoxin; Similar to GB:AE000666 percent identity: 37.01; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.524 |
MJ_0934 | MJ_0514.2 | MJ_0934 | MJ_0514.2 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Polyferredoxin; Similar to GB:AE000666 percent identity: 37.01; identified by sequence similarity; putative. | 0.524 |
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 | MJ_1068 | MJ_0934 | MJ_1068 | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | Polysaccharide biosynthesis protein (capF) isolog; Similar to GB:U10927 SP:P39855 PID:506702 percent identity: 21.66; identified by sequence similarity; putative. | 0.419 |
MJ_0934 | MJ_1141 | MJ_0934 | MJ_1141 | 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: 38.92; identified by sequence similarity; putative. | 0.472 |
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_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 |
MJ_1068 | MJ_0934 | MJ_1068 | MJ_0934 | Polysaccharide biosynthesis protein (capF) isolog; Similar to GB:U10927 SP:P39855 PID:506702 percent identity: 21.66; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.419 |
MJ_1141 | MJ_0934 | MJ_1141 | MJ_0934 | Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 38.92; identified by sequence similarity; putative. | Polyferredoxin (mvhB); Similar to GB:M34016 PID:149806 percent identity: 40.85; identified by sequence similarity; putative. | 0.472 |
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 |