| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EAQ05421.1 | def | SKA53_03394 | SKA53_09974 | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.404 |
| EAQ05421.1 | fhs | SKA53_03394 | SKA53_08541 | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | Formate--tetrahydrofolate ligase; COG2759 Formyltetrahydrofolate synthetase; Belongs to the formate--tetrahydrofolate ligase family. | 0.961 |
| EAQ05421.1 | fmt | SKA53_03394 | SKA53_09969 | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.889 |
| EAQ05421.1 | folD | SKA53_03394 | SKA53_08536 | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | folD bifunctional protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.976 |
| EAQ05421.1 | metG | SKA53_03394 | SKA53_01331 | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.415 |
| EAQ05421.1 | purH | SKA53_03394 | SKA53_12688 | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful). | 0.999 |
| def | EAQ05421.1 | SKA53_09974 | SKA53_03394 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | 0.404 |
| def | def-2 | SKA53_09974 | SKA53_09979 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.825 |
| def | def-3 | SKA53_09974 | SKA53_09984 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.801 |
| def | fmt | SKA53_09974 | SKA53_09969 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.924 |
| def-2 | def | SKA53_09979 | SKA53_09974 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.825 |
| def-2 | def-3 | SKA53_09979 | SKA53_09984 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.793 |
| def-2 | fmt | SKA53_09979 | SKA53_09969 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.945 |
| def-3 | def | SKA53_09984 | SKA53_09974 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Belongs to the polypeptide deformylase family. | 0.801 |
| def-3 | def-2 | SKA53_09984 | SKA53_09979 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | 0.793 |
| def-3 | fmt | SKA53_09984 | SKA53_09969 | Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.955 |
| fhs | EAQ05421.1 | SKA53_08541 | SKA53_03394 | Formate--tetrahydrofolate ligase; COG2759 Formyltetrahydrofolate synthetase; Belongs to the formate--tetrahydrofolate ligase family. | COG0299 Folate-dependent phosphoribosylglycinamide formyltransferase PurN. | 0.961 |
| fhs | fmt | SKA53_08541 | SKA53_09969 | Formate--tetrahydrofolate ligase; COG2759 Formyltetrahydrofolate synthetase; Belongs to the formate--tetrahydrofolate ligase family. | methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. | 0.897 |
| fhs | folD | SKA53_08541 | SKA53_08536 | Formate--tetrahydrofolate ligase; COG2759 Formyltetrahydrofolate synthetase; Belongs to the formate--tetrahydrofolate ligase family. | folD bifunctional protein; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.998 |
| fhs | purH | SKA53_08541 | SKA53_12688 | Formate--tetrahydrofolate ligase; COG2759 Formyltetrahydrofolate synthetase; Belongs to the formate--tetrahydrofolate ligase family. | Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; COG0138 AICAR transformylase/IMP cyclohydrolase PurH (only IMP cyclohydrolase domain in Aful). | 0.982 |