| 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. | 0.693 |
| 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 | exbD3 | azo0618 | azo0613 | Putative hemin uptake protein; 47% DUF1008. Pfam:PF06228; DUF1008; 1; High confidence in function and specificity. | Probable fiopolymer transport protein ExbD. Homology to exbD1 of X. campestris of 43%. ExbD is part of the TonB-dependent transduction complex. The TonB complex uses the proton gradient across the inner bacterial membrane to transport large molecules across the outer bacterial membrane. InterPro: Biopolymer transport protein ExbD/TolR Pfam: Biopolymer transport protein ExbD/TolR no signal peptide probable 1 TMH; High confidence in function and specificity. | 0.431 |
| 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. | 0.417 |
| 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. | 0.693 |
| 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. | 0.842 |
| 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. | 0.962 |
| 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. | 0.764 |
| 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). | 0.690 |
| bfd | cysI | azo0617 | azo0432 | 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 sulfite reductase; 49% Fd-NiR.IPR011255; NiR_SiRalpha_1/3.IPR006067; Nir_Sir_4Fe4S.IPR005117; NiR_SiR_beta_fer. Pfam:PF01077; NIR_SIR; 2.PF03460; NIR_SIR_ferr; 2; High confidence in function and specificity. | 0.607 |
| bfd | exbB2 | azo0617 | azo0614 | 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 biopolymer transport protein ExbB. Homology to exbB of B. pertussis of 50% ExbB is part of the TonB-dependent transduction complex. The TonB complex uses the proton gradient across the inner bacterial membrane to transport large molecules across the outer bacterial membrane. InterPro: MotA/TolQ/ExbB proton channel family Pfam: MotA/TolQ/ExbB proton channel family no signal peptide no TMHs; Family membership. | 0.582 |
| bfd | exbD3 | azo0617 | azo0613 | 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 fiopolymer transport protein ExbD. Homology to exbD1 of X. campestris of 43%. ExbD is part of the TonB-dependent transduction complex. The TonB complex uses the proton gradient across the inner bacterial membrane to transport large molecules across the outer bacterial membrane. InterPro: Biopolymer transport protein ExbD/TolR Pfam: Biopolymer transport protein ExbD/TolR no signal peptide probable 1 TMH; High confidence in function and specificity. | 0.580 |
| 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 [...] | 0.626 |
| 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. | 0.608 |
| 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. | 0.842 |
| 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. | 0.545 |
| 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. | 0.962 |
| 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. | 0.566 |
| bfr2 | exbB2 | azo0616 | azo0614 | Putative bacterioferritin; Iron-storage protein. | Probable biopolymer transport protein ExbB. Homology to exbB of B. pertussis of 50% ExbB is part of the TonB-dependent transduction complex. The TonB complex uses the proton gradient across the inner bacterial membrane to transport large molecules across the outer bacterial membrane. InterPro: MotA/TolQ/ExbB proton channel family Pfam: MotA/TolQ/ExbB proton channel family no signal peptide no TMHs; Family membership. | 0.421 |