| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bfr | hemH | DR95_2145 | DR95_3445 | 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. | 0.913 |
| cyaY | hemH | DR95_3341 | DR95_3445 | Iron donor protein CyaY; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.830 |
| cyoE | hemH | DR95_1817 | DR95_3445 | 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. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.925 |
| fadB | fadJ | DR95_3514 | DR95_151 | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | Fatty oxidation complex, alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.991 |
| fadB | hemG | DR95_3514 | DR95_3510 | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | Flavodoxin domain protein. | 0.461 |
| fadB | hemH | DR95_3514 | DR95_3445 | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.822 |
| fadB | lon | DR95_3514 | DR95_1804 | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.880 |
| fadJ | fadB | DR95_151 | DR95_3514 | Fatty oxidation complex, alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | Fatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 0.991 |
| fadJ | hemH | DR95_151 | DR95_3445 | Fatty oxidation complex, alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.822 |
| fadJ | lon | DR95_151 | DR95_1804 | Fatty oxidation complex, alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.880 |
| hemC | hemE | DR95_3343 | DR95_2773 | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | hemE: uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. | 0.990 |
| hemC | hemF | DR95_3343 | DR95_109 | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Coproporphyrinogen III oxidase family protein; 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. | 0.673 |
| hemC | hemG | DR95_3343 | DR95_3510 | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Flavodoxin domain protein. | 0.485 |
| hemC | hemH | DR95_3343 | DR95_3445 | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.709 |
| hemE | hemC | DR95_2773 | DR95_3343 | hemE: uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | 0.990 |
| hemE | hemF | DR95_2773 | DR95_109 | hemE: uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. | Coproporphyrinogen III oxidase family protein; 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. | 0.972 |
| hemE | hemH | DR95_2773 | DR95_3445 | hemE: uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. | 0.919 |
| hemF | hemC | DR95_109 | DR95_3343 | Coproporphyrinogen III oxidase family protein; 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. | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | 0.673 |
| hemF | hemE | DR95_109 | DR95_2773 | Coproporphyrinogen III oxidase family protein; 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. | hemE: uroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. | 0.972 |
| hemF | hemG | DR95_109 | DR95_3510 | Coproporphyrinogen III oxidase family protein; 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. | Flavodoxin domain protein. | 0.944 |