| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKL33365.1 | bfr | AB185_05295 | AB185_09365 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0337 (CsbD) family. | 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. | 0.460 |
| AKL33365.1 | dps | AB185_05295 | AB185_27005 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0337 (CsbD) 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. | 0.450 |
| aroD | bfr | AB185_31620 | AB185_09365 | 3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. Belongs to the type-I 3-dehydroquinase family. | 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. | 0.470 |
| bfd | bfr | AB185_09360 | AB185_09365 | Bacterioferritin-associated ferredoxin; 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. | 0.967 |
| bfr | AKL33365.1 | AB185_09365 | AB185_05295 | 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; Belongs to the UPF0337 (CsbD) family. | 0.460 |
| bfr | aroD | AB185_09365 | AB185_31620 | 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. | 3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. Belongs to the type-I 3-dehydroquinase family. | 0.470 |
| bfr | bfd | AB185_09365 | AB185_09360 | 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-associated ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.967 |
| bfr | dps | AB185_09365 | AB185_27005 | 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. | 0.560 |
| bfr | hemH | AB185_09365 | AB185_29220 | 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. | 0.922 |
| bfr | nasA | AB185_09365 | AB185_18740 | 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; Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | 0.691 |
| bfr | norV | AB185_09365 | AB185_13325 | 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. | Nitric oxide reductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. | 0.477 |
| bfr | nuoC | AB185_09365 | AB185_15730 | 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:ubiquinone oxidoreductase; 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. | 0.542 |
| bfr | psiF | AB185_09365 | AB185_29885 | 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. | 0.491 |
| bfr | zur | AB185_09365 | AB185_05290 | 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. | Zinc uptake transcriptional repressor; Acts as a negative controlling element, employing Zn(2+) as a cofactor to bind the operator of the repressed genes znuACB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Fur family. | 0.455 |
| dps | AKL33365.1 | AB185_27005 | AB185_05295 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0337 (CsbD) family. | 0.450 |
| dps | bfr | AB185_27005 | AB185_09365 | 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. | 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. | 0.560 |
| hemH | bfr | AB185_29220 | AB185_09365 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 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. | 0.922 |
| nasA | bfr | AB185_18740 | AB185_09365 | Nitrate reductase; Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | 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. | 0.691 |
| norV | bfr | AB185_13325 | AB185_09365 | Nitric oxide reductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. | 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. | 0.477 |
| norV | nuoC | AB185_13325 | AB185_15730 | Nitric oxide reductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. | NADH:ubiquinone oxidoreductase; 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. | 0.579 |
