| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa1021 | dacA | PSHAa1021 | PSHAa1022 | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase S11 family. | 0.742 |
| PSHAa1021 | lipA | PSHAa1021 | PSHAa1019 | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.934 |
| PSHAa1021 | lipB | PSHAa1021 | PSHAa1020 | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.953 |
| PSHAa1021 | mrdA | PSHAa1021 | PSHAa1025 | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | Cell elongation-specific transpeptidase of penicillin-binding protein 2 (peptidoglycan synthetase); Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily. | 0.599 |
| PSHAa1021 | nfuA | PSHAa1021 | PSHAa2860 | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | Conserved protein of unknown function; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. | 0.455 |
| PSHAa1021 | rlpA | PSHAa1021 | PSHAa1023 | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | Putative Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.634 |
| PSHAa1385 | lipA | PSHAa1385 | PSHAa1019 | Putative esterase; Serine hydrolase involved in the detoxification of formaldehyde. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.705 |
| birA | gcvH | PSHAa2913 | PSHAa2474 | Biotin-[protein] holoenzyme synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | 0.576 |
| birA | gcvP | PSHAa2913 | PSHAa2473 | Biotin-[protein] holoenzyme synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Glycine cleavage complex protein P, glycine decarboxylase, PLP-dependent; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.576 |
| birA | lipA | PSHAa2913 | PSHAa1019 | Biotin-[protein] holoenzyme synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.601 |
| birA | lipB | PSHAa2913 | PSHAa1020 | Biotin-[protein] holoenzyme synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.602 |
| dacA | PSHAa1021 | PSHAa1022 | PSHAa1021 | D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase S11 family. | Homologs of previously reported genes of unknown function; Belongs to the UPF0250 family. | 0.742 |
| dacA | lipA | PSHAa1022 | PSHAa1019 | D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase S11 family. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.700 |
| dacA | lipB | PSHAa1022 | PSHAa1020 | D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase S11 family. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.768 |
| dacA | mrdA | PSHAa1022 | PSHAa1025 | D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase S11 family. | Cell elongation-specific transpeptidase of penicillin-binding protein 2 (peptidoglycan synthetase); Catalyzes cross-linking of the peptidoglycan cell wall. Belongs to the transpeptidase family. MrdA subfamily. | 0.997 |
| dacA | rlpA | PSHAa1022 | PSHAa1023 | D-alanyl-D-alanine carboxypeptidase, penicillin-binding protein 5; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the peptidase S11 family. | Putative Rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.734 |
| gcvH | birA | PSHAa2474 | PSHAa2913 | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Biotin-[protein] holoenzyme synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | 0.576 |
| gcvH | gcvP | PSHAa2474 | PSHAa2473 | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Glycine cleavage complex protein P, glycine decarboxylase, PLP-dependent; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.999 |
| gcvH | lipA | PSHAa2474 | PSHAa1019 | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | 0.934 |
| gcvH | lipB | PSHAa2474 | PSHAa1020 | Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | 0.878 |
