| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| def | fmt | BL02297 | BL02298 | Polypeptide 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 Fmt; 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. | 0.991 |
| def | priA | BL02297 | BL02296 | Polypeptide 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. | Primosomal replication factor Y (primosomal protein N'); Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.767 |
| def | prpC | BL02297 | BL02301 | Polypeptide 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. | Protein phosphatase. | 0.841 |
| def | rsmB | BL02297 | BL02299 | Polypeptide 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. | rRNA SAM-dependent methyltransferase RmsB; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.870 |
| def | yloN | BL02297 | BL02300 | Polypeptide 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. | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. | 0.885 |
| fhs | fmt | BL01370 | BL02298 | Formate tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | methionyl-tRNA formyltransferase Fmt; 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. | 0.932 |
| fhs | purH | BL01370 | BL01486 | Formate tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Phosphoribosylaminoimidazole carboxy formyl formyltransferase and inosine-monophosphate cyclohydrolase. | 0.987 |
| fhs | purN | BL01370 | BL01485 | Formate tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. | 0.980 |
| fhs | purU | BL01370 | BL03753 | Formate tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). | 0.917 |
| fhs | rsmB | BL01370 | BL02299 | Formate tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | rRNA SAM-dependent methyltransferase RmsB; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.637 |
| fmt | def | BL02298 | BL02297 | methionyl-tRNA formyltransferase Fmt; 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. | Polypeptide 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. | 0.991 |
| fmt | fhs | BL02298 | BL01370 | methionyl-tRNA formyltransferase Fmt; 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. | Formate tetrahydrofolate ligase; Belongs to the formate--tetrahydrofolate ligase family. | 0.932 |
| fmt | metS | BL02298 | BL00533 | methionyl-tRNA formyltransferase Fmt; 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. | methionyl-tRNA synthetase MetS; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. | 0.943 |
| fmt | priA | BL02298 | BL02296 | methionyl-tRNA formyltransferase Fmt; 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. | Primosomal replication factor Y (primosomal protein N'); Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. | 0.957 |
| fmt | prpC | BL02298 | BL02301 | methionyl-tRNA formyltransferase Fmt; 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. | Protein phosphatase. | 0.982 |
| fmt | purH | BL02298 | BL01486 | methionyl-tRNA formyltransferase Fmt; 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. | Phosphoribosylaminoimidazole carboxy formyl formyltransferase and inosine-monophosphate cyclohydrolase. | 0.919 |
| fmt | purN | BL02298 | BL01485 | methionyl-tRNA formyltransferase Fmt; 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. | Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. | 0.924 |
| fmt | purU | BL02298 | BL03753 | methionyl-tRNA formyltransferase Fmt; 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. | Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). | 0.900 |
| fmt | rsmB | BL02298 | BL02299 | methionyl-tRNA formyltransferase Fmt; 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. | rRNA SAM-dependent methyltransferase RmsB; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. | 0.998 |
| fmt | yloN | BL02298 | BL02300 | methionyl-tRNA formyltransferase Fmt; 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. | Conserved hypothetical protein; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. | 0.939 |