| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0618 | bfd | azo0618 | azo0617 | Putative hemin uptake protein; 47% DUF1008. Pfam:PF06228; DUF1008; 1; High confidence in function and specificity. | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | 0.719 |
| azo0618 | bfr2 | azo0618 | azo0616 | Putative hemin uptake protein; 47% DUF1008. Pfam:PF06228; DUF1008; 1; High confidence in function and specificity. | Putative bacterioferritin; Iron-storage protein. | 0.663 |
| azo0618 | tonB1 | azo0618 | azo0615 | Putative hemin uptake protein; 47% DUF1008. Pfam:PF06228; DUF1008; 1; High confidence in function and specificity. | Putative TonB protein. Homology to tonb2 of P. aeruginosa of 39% (TREMBL:Q9RMT3). To complete transport of bound iron across the inner membrane, a second receptor complex is needed. The major component of this is tonB, a 27kDa protein that facilitates energy transfer from the proton motive force to outer receptors Pfam: Gram-negative bacterial TonB protein no signal peptide 1 TMH; Function unclear. | 0.424 |
| bfd | azo0618 | azo0617 | azo0618 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Putative hemin uptake protein; 47% DUF1008. Pfam:PF06228; DUF1008; 1; High confidence in function and specificity. | 0.719 |
| bfd | bfr1 | azo0617 | azo0247 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Putative bacterioferritin; Iron-storage protein. | 0.897 |
| bfd | bfr2 | azo0617 | azo0616 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Putative bacterioferritin; Iron-storage protein. | 0.975 |
| bfd | bfr3 | azo0617 | azo1784 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome B-557). In E. coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter.X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryota and prokaryota. Key role in iron homeostasis.InterPro: Bacterioferritin. Non-secretory protein bfr: bacterioferritin; High confidence in function and specificity. | 0.842 |
| bfd | coxB | azo0617 | azo3304 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Conserved hypothetical cytochrome c oxidase,subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.692 |
| bfd | gcvP | azo0617 | azo1285 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Glycine cleavage system P-protein; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. | 0.668 |
| bfd | gltB | azo0617 | azo3642 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Ferredoxin-dependent glutamate synthase,; Specificity unclear. | 0.930 |
| bfd | narK | azo0617 | azo1288 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Probable nitrate transporters are involved in excretion of nitrite produced by the dissimilatory reduction of nitrate. NarK is polytopic membrane protein with 12 transmembrane domains which is involved in nitrate uptake and nitrite excretion and is thought to function as a nitrate/nitrite antiporter. At low concentrations of nitrate, NarK mediates the electrogenic excretion of nitrite rather than nitrate/nitrite exchange., 90% similarity to a probable nitrate transporter protein in Azoarcus sp. EbN1., InterPRo:04737: nitrate transporter,Signal peptide no present, TMHx:12, ; High confid [...] | 0.608 |
| bfd | nifU | azo0617 | azo0553 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Probable nitrogen fixation protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. | 0.630 |
| bfd | tonB1 | azo0617 | azo0615 | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | Putative TonB protein. Homology to tonb2 of P. aeruginosa of 39% (TREMBL:Q9RMT3). To complete transport of bound iron across the inner membrane, a second receptor complex is needed. The major component of this is tonB, a 27kDa protein that facilitates energy transfer from the proton motive force to outer receptors Pfam: Gram-negative bacterial TonB protein no signal peptide 1 TMH; Function unclear. | 0.618 |
| bfr1 | bfd | azo0247 | azo0617 | Putative bacterioferritin; Iron-storage protein. | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | 0.897 |
| bfr1 | bfr3 | azo0247 | azo1784 | Putative bacterioferritin; Iron-storage protein. | Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome B-557). In E. coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter.X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryota and prokaryota. Key role in iron homeostasis.InterPro: Bacterioferritin. Non-secretory protein bfr: bacterioferritin; High confidence in function and specificity. | 0.543 |
| bfr2 | azo0618 | azo0616 | azo0618 | Putative bacterioferritin; Iron-storage protein. | Putative hemin uptake protein; 47% DUF1008. Pfam:PF06228; DUF1008; 1; High confidence in function and specificity. | 0.663 |
| bfr2 | bfd | azo0616 | azo0617 | Putative bacterioferritin; Iron-storage protein. | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | 0.975 |
| bfr2 | bfr3 | azo0616 | azo1784 | Putative bacterioferritin; Iron-storage protein. | Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome B-557). In E. coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter.X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryota and prokaryota. Key role in iron homeostasis.InterPro: Bacterioferritin. Non-secretory protein bfr: bacterioferritin; High confidence in function and specificity. | 0.565 |
| bfr2 | tonB1 | azo0616 | azo0615 | Putative bacterioferritin; Iron-storage protein. | Putative TonB protein. Homology to tonb2 of P. aeruginosa of 39% (TREMBL:Q9RMT3). To complete transport of bound iron across the inner membrane, a second receptor complex is needed. The major component of this is tonB, a 27kDa protein that facilitates energy transfer from the proton motive force to outer receptors Pfam: Gram-negative bacterial TonB protein no signal peptide 1 TMH; Function unclear. | 0.425 |
| bfr3 | bfd | azo1784 | azo0617 | Bacterioferritin (BFR) (Cytochrome B-1) (Cytochrome B-557). In E. coli is an iron-storage protein consisting of 24 identical subunits that pack together to form a highly symmetrical, nearly spherical shell surrounding a central cavity of about 8 nm diameter.X-ray crystallographic studies have revealed a close structural similarity between BFR and the ferritins, a family of iron-storage proteins found in both eukaryota and prokaryota. Key role in iron homeostasis.InterPro: Bacterioferritin. Non-secretory protein bfr: bacterioferritin; High confidence in function and specificity. | Bacterioferritin-associated ferredoxin. Homology to psto4159 of P. syringae of 33% (trembl|Q87XL9). SEEMS TO ASSOCIATE WITH BFR; COULD BE A GENERAL REDOX AND/OR REGULATORY COMPONENT PARTICIPATING IN THE IRON STORAGE MOBILIZATION FUNCTIONS OF BFR. COULD PARTICIPATE IN THE RELEASE OR THE DELIVERY OF IRON FROM/TO BACTERIOFERRITIN (OR OTHER IRON COMPLEXES). Pfam: BFD-like [2Fe-2S] binding domain no signal peptide no TMHs; Conserved hypothetical protein. | 0.842 |