| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJC45243.1 | hemF | SB85_05220 | SB85_12215 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. | 0.948 |
| AJC45243.1 | hemH | SB85_05220 | SB85_12100 | Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.951 |
| AJC45614.1 | AJC47736.1 | SB85_07325 | SB85_17620 | Bacterioferritin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heme oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| AJC45614.1 | bfr | SB85_07325 | SB85_05025 | 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. | 0.913 |
| AJC45614.1 | bfr-2 | SB85_07325 | SB85_11100 | 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. | 0.907 |
| AJC45614.1 | hemH | SB85_07325 | SB85_12100 | Bacterioferritin; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.909 |
| AJC46387.1 | hemH | SB85_12095 | SB85_12100 | Hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.848 |
| AJC46751.1 | hemC | SB85_14365 | SB85_16455 | Delta-aminolevulinic acid dehydratase; Catalyzes the formation of porphobilinogen from 5-aminolevulinate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ALAD family. | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | 0.997 |
| AJC46751.1 | hemF | SB85_14365 | SB85_12215 | Delta-aminolevulinic acid dehydratase; Catalyzes the formation of porphobilinogen from 5-aminolevulinate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ALAD family. | Coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. | 0.659 |
| AJC46751.1 | hemH | SB85_14365 | SB85_12100 | Delta-aminolevulinic acid dehydratase; Catalyzes the formation of porphobilinogen from 5-aminolevulinate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ALAD family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.679 |
| AJC47736.1 | AJC45614.1 | SB85_17620 | SB85_07325 | Heme oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Bacterioferritin; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| AJC47736.1 | bfr | SB85_17620 | SB85_05025 | Heme oxygenase; 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. | 0.900 |
| AJC47736.1 | bfr-2 | SB85_17620 | SB85_11100 | Heme oxygenase; 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. | 0.900 |
| AJC47736.1 | cyoE | SB85_17620 | SB85_15120 | Heme oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. | 0.900 |
| AJC47736.1 | hemH | SB85_17620 | SB85_12100 | Heme oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.904 |
| bfr | AJC45614.1 | SB85_05025 | SB85_07325 | 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. | 0.913 |
| bfr | AJC47736.1 | SB85_05025 | SB85_17620 | 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. | Heme oxygenase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.900 |
| bfr | bfr-2 | SB85_05025 | SB85_11100 | 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; 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. | 0.914 |
| bfr | hemH | SB85_05025 | SB85_12100 | 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. | 0.909 |
| bfr-2 | AJC45614.1 | SB85_11100 | SB85_07325 | 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. | 0.907 |