node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
FRAAL5224 | def | FRAAL5224 | FRAAL0019 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Peptide deformylase 3 (PDF 3) (Polypeptide deformylase 3); 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. | 0.581 |
FRAAL5224 | def-2 | FRAAL5224 | FRAAL2799 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Peptide deformylase 2 (PDF 2) (Polypeptide deformylase 2); 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. | 0.626 |
FRAAL5224 | fmt | FRAAL5224 | FRAAL5225 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | 0.997 |
FRAAL5224 | folD | FRAAL5224 | FRAAL2298 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.640 |
FRAAL5224 | folD-2 | FRAAL5224 | FRAAL4216 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | Bifunctional: 5,10-methylene-tetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.640 |
FRAAL5224 | purN | FRAAL5224 | FRAAL1161 | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP 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. | 0.442 |
def | FRAAL5224 | FRAAL0019 | FRAAL5224 | Peptide deformylase 3 (PDF 3) (Polypeptide deformylase 3); 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; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.581 |
def | fmt | FRAAL0019 | FRAAL5225 | Peptide deformylase 3 (PDF 3) (Polypeptide deformylase 3); 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. | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | 0.942 |
def | gcvT | FRAAL0019 | FRAAL5148 | Peptide deformylase 3 (PDF 3) (Polypeptide deformylase 3); 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. | Aminomethyltransferase (Glycine cleavage system T protein); The glycine cleavage system catalyzes the degradation of glycine. | 0.426 |
def-2 | FRAAL5224 | FRAAL2799 | FRAAL5224 | Peptide deformylase 2 (PDF 2) (Polypeptide deformylase 2); 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; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.626 |
def-2 | fmt | FRAAL2799 | FRAAL5225 | Peptide deformylase 2 (PDF 2) (Polypeptide deformylase 2); 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. | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | 0.966 |
fmt | FRAAL5224 | FRAAL5225 | FRAAL5224 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Conserved hypothetical protein; Homologs of previously reported genes of unknown function; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. | 0.997 |
fmt | def | FRAAL5225 | FRAAL0019 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Peptide deformylase 3 (PDF 3) (Polypeptide deformylase 3); 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. | 0.942 |
fmt | def-2 | FRAAL5225 | FRAAL2799 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Peptide deformylase 2 (PDF 2) (Polypeptide deformylase 2); 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. | 0.966 |
fmt | folD | FRAAL5225 | FRAAL2298 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.966 |
fmt | folD-2 | FRAAL5225 | FRAAL4216 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Bifunctional: 5,10-methylene-tetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.963 |
fmt | gcvT | FRAAL5225 | FRAAL5148 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Aminomethyltransferase (Glycine cleavage system T protein); The glycine cleavage system catalyzes the degradation of glycine. | 0.956 |
fmt | glyA | FRAAL5225 | FRAAL1125 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.946 |
fmt | glyA-2 | FRAAL5225 | FRAAL5942 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | Serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | 0.946 |
fmt | purN | FRAAL5225 | FRAAL1161 | 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-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. | 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. | 0.956 |