| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| hemE | hemH | BSU10120 | BSU10130 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | 0.999 |
| hemE | hemQ | BSU10120 | BSU37670 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | 0.853 |
| hemE | hemY | BSU10120 | BSU10140 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | 0.999 |
| hemE | hmoA | BSU10120 | BSU07150 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Heme-degrading monooxygenase; Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.647 |
| hemE | hmoB | BSU10120 | BSU10100 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.879 |
| hemE | yhfA | BSU10120 | BSU10080 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter. | 0.465 |
| hemE | yhgD | BSU10120 | BSU10150 | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.469 |
| hemH | hemE | BSU10130 | BSU10120 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.999 |
| hemH | hemQ | BSU10130 | BSU37670 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | 0.998 |
| hemH | hemY | BSU10130 | BSU10140 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | 0.999 |
| hemH | hmoA | BSU10130 | BSU07150 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | Heme-degrading monooxygenase; Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.925 |
| hemH | hmoB | BSU10130 | BSU10100 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.724 |
| hemH | yhgD | BSU10130 | BSU10150 | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | Putative transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. | 0.585 |
| hemQ | hemE | BSU37670 | BSU10120 | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.853 |
| hemQ | hemH | BSU37670 | BSU10130 | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. | 0.998 |
| hemQ | hemY | BSU37670 | BSU10140 | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | 0.993 |
| hemQ | hmoA | BSU37670 | BSU07150 | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | Heme-degrading monooxygenase; Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.970 |
| hemQ | hmoB | BSU37670 | BSU10100 | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | Heme-degrading monooxygenase; Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. | 0.755 |
| hemQ | yqjZ | BSU37670 | BSU23680 | Essential component of heme biosynthesis; May function as heme-dependent peroxidase. | Putative degradation enzyme (oxygenase); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. | 0.903 |
| hemY | hemE | BSU10140 | BSU10120 | Protoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. | Uroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | 0.999 |