| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PSHAa0953 | PSHAa1823 | PSHAa0953 | PSHAa1823 | Putative anti-sigma factor antagonist; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; factor; Belongs to the anti-sigma-factor antagonist family. | Homologs of previously reported genes of unknown function. | 0.662 |
| PSHAa0953 | bfr | PSHAa0953 | PSHAb0283 | Putative anti-sigma factor antagonist; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; factor; Belongs to the anti-sigma-factor antagonist family. | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.592 |
| PSHAa0953 | bfr-2 | PSHAa0953 | PSHAb0284 | Putative anti-sigma factor antagonist; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; factor; Belongs to the anti-sigma-factor antagonist family. | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.592 |
| PSHAa1822 | PSHAa1823 | PSHAa1822 | PSHAa1823 | Putative transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | Homologs of previously reported genes of unknown function. | 0.468 |
| PSHAa1822 | aceK2 | PSHAa1822 | PSHAa1821 | Putative transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.786 |
| PSHAa1823 | PSHAa0953 | PSHAa1823 | PSHAa0953 | Homologs of previously reported genes of unknown function. | Putative anti-sigma factor antagonist; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; factor; Belongs to the anti-sigma-factor antagonist family. | 0.662 |
| PSHAa1823 | PSHAa1822 | PSHAa1823 | PSHAa1822 | Homologs of previously reported genes of unknown function. | Putative transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | 0.468 |
| PSHAa1823 | PSHAa2218 | PSHAa1823 | PSHAa2218 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function; Belongs to the UPF0337 (CsbD) family. | 0.452 |
| PSHAa1823 | PSHAa2964 | PSHAa1823 | PSHAa2964 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.537 |
| PSHAa1823 | aceK2 | PSHAa1823 | PSHAa1821 | Homologs of previously reported genes of unknown function. | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | 0.440 |
| PSHAa1823 | bfr | PSHAa1823 | PSHAb0283 | Homologs of previously reported genes of unknown function. | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.563 |
| PSHAa1823 | bfr-2 | PSHAa1823 | PSHAb0284 | Homologs of previously reported genes of unknown function. | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.563 |
| PSHAa2218 | PSHAa1823 | PSHAa2218 | PSHAa1823 | Homologs of previously reported genes of unknown function; Belongs to the UPF0337 (CsbD) family. | Homologs of previously reported genes of unknown function. | 0.452 |
| PSHAa2964 | PSHAa1823 | PSHAa2964 | PSHAa1823 | Homologs of previously reported genes of unknown function. | Homologs of previously reported genes of unknown function. | 0.537 |
| aceK2 | PSHAa1822 | PSHAa1821 | PSHAa1822 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Putative transcriptional regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; regulator; Belongs to the LysR transcriptional regulatory family. | 0.786 |
| aceK2 | PSHAa1823 | PSHAa1821 | PSHAa1823 | Putative isocitrate dehydrogenase kinase/phosphatase; Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | Homologs of previously reported genes of unknown function. | 0.440 |
| bfr | PSHAa0953 | PSHAb0283 | PSHAa0953 | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Putative anti-sigma factor antagonist; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; factor; Belongs to the anti-sigma-factor antagonist family. | 0.592 |
| bfr | PSHAa1823 | PSHAb0283 | PSHAa1823 | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Homologs of previously reported genes of unknown function. | 0.563 |
| bfr | bfr-2 | PSHAb0283 | PSHAb0284 | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | 0.986 |
| bfr-2 | PSHAa0953 | PSHAb0284 | PSHAa0953 | Bacterioferritin (Cytochrome B-1) (Cytochrome B-557); Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. | Putative anti-sigma factor antagonist; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; factor; Belongs to the anti-sigma-factor antagonist family. | 0.592 |