| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AOE40078.1 | AOE40079.1 | BEE12_09570 | BEE12_09575 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Stress protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.774 |
| AOE40078.1 | bfr_2 | BEE12_09570 | BEE12_04940 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; 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. | 0.447 |
| AOE40079.1 | AOE40078.1 | BEE12_09575 | BEE12_09570 | Stress protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.774 |
| AOE40079.1 | bfr_2 | BEE12_09575 | BEE12_04940 | Stress protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; 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. | 0.447 |
| AOE41073.1 | arcB | BEE12_15150 | BEE12_09050 | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Aerobic respiration two-component sensor histidine kinase ArcB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.443 |
| AOE41073.1 | bfr_2 | BEE12_15150 | BEE12_04940 | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; 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. | 0.793 |
| AOE41073.1 | nuoC | BEE12_15150 | BEE12_01095 | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.436 |
| arcB | AOE41073.1 | BEE12_09050 | BEE12_15150 | Aerobic respiration two-component sensor histidine kinase ArcB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.443 |
| arcB | bfr_2 | BEE12_09050 | BEE12_04940 | Aerobic respiration two-component sensor histidine kinase ArcB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; 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. | 0.465 |
| arcB | cheV | BEE12_09050 | BEE12_11160 | Aerobic respiration two-component sensor histidine kinase ArcB; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chemotaxis protein CheV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.995 |
| bfd | bfr_2 | BEE12_04945 | BEE12_04940 | Bacterioferritin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; 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. | 0.915 |
| bfr_2 | AOE40078.1 | BEE12_04940 | BEE12_09570 | Bacterioferritin; 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.447 |
| bfr_2 | AOE40079.1 | BEE12_04940 | BEE12_09575 | Bacterioferritin; 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. | Stress protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.447 |
| bfr_2 | AOE41073.1 | BEE12_04940 | BEE12_15150 | Bacterioferritin; 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. | Nitrate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.793 |
| bfr_2 | arcB | BEE12_04940 | BEE12_09050 | Bacterioferritin; 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. | Aerobic respiration two-component sensor histidine kinase ArcB; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.465 |
| bfr_2 | bfd | BEE12_04940 | BEE12_04945 | Bacterioferritin; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.915 |
| bfr_2 | cheV | BEE12_04940 | BEE12_11160 | Bacterioferritin; 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. | Chemotaxis protein CheV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.453 |
| bfr_2 | dps | BEE12_04940 | BEE12_13105 | Bacterioferritin; 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. | DNA starvation/stationary phase protection protein Dps; During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction; Belongs to the Dps family. | 0.447 |
| bfr_2 | hemH_1 | BEE12_04940 | BEE12_11785 | Bacterioferritin; 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. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.928 |
| bfr_2 | nuoC | BEE12_04940 | BEE12_01095 | Bacterioferritin; 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. | NADH-quinone oxidoreductase subunit C/D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.422 |