| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Smon_0370 | def | Smon_0370 | Smon_0372 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | 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. | 0.795 |
| Smon_0370 | fmt | Smon_0370 | Smon_0373 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | 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. | 0.774 |
| Smon_0370 | folD | Smon_0370 | Smon_0375 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | Methylenetetrahydrofolate dehydrogenase (NADP(+)); Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.746 |
| Smon_0370 | gatA | Smon_0370 | Smon_0368 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | glutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.790 |
| Smon_0370 | gatB | Smon_0370 | Smon_0369 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.805 |
| Smon_0370 | gatC | Smon_0370 | Smon_0367 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.823 |
| Smon_0370 | priA | Smon_0370 | Smon_0371 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | 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. | 0.775 |
| Smon_0370 | rex | Smon_0370 | Smon_0374 | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | CoA-binding domain protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | 0.747 |
| Smon_0739 | Smon_1480 | Smon_0739 | Smon_1480 | Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; KEGG: bcb:BCB4264_A2176 single-stranded DNA-binding protein. | 0.656 |
| Smon_0739 | priA | Smon_0739 | Smon_0371 | Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | 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. | 0.603 |
| Smon_1480 | Smon_0739 | Smon_1480 | Smon_0739 | TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; KEGG: bcb:BCB4264_A2176 single-stranded DNA-binding protein. | Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. | 0.656 |
| Smon_1480 | priA | Smon_1480 | Smon_0371 | TIGRFAM: single-strand binding protein; PFAM: single-strand binding protein/Primosomal replication protein n; KEGG: bcb:BCB4264_A2176 single-stranded DNA-binding protein. | 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. | 0.866 |
| def | Smon_0370 | Smon_0372 | Smon_0370 | 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. | Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein transpeptidase; PASTA domain containing protein; Penicillin-binding protein dimerisation domain; KEGG: gme:Gmet_0406 penicillin-binding protein, transpeptidase. | 0.795 |
| def | fmt | Smon_0372 | Smon_0373 | 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. | 0.984 |
| def | folD | Smon_0372 | Smon_0375 | 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. | Methylenetetrahydrofolate dehydrogenase (NADP(+)); Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. | 0.882 |
| def | gatA | Smon_0372 | Smon_0368 | 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. | glutamyl-tRNA(Gln) amidotransferase, A subunit; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). | 0.731 |
| def | gatB | Smon_0372 | Smon_0369 | 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. | glutamyl-tRNA(Gln) amidotransferase, B subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. | 0.763 |
| def | gatC | Smon_0372 | Smon_0367 | 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. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.743 |
| def | priA | Smon_0372 | Smon_0371 | 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. | 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. | 0.822 |
| def | rex | Smon_0372 | Smon_0374 | 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. | CoA-binding domain protein; Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | 0.801 |