| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| azo0524 | azo0525 | azo0524 | azo0525 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | 0.553 |
| azo0524 | fdh1B | azo0524 | azo3039 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity. | 0.996 |
| azo0524 | fdxC | azo0524 | azo0527 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Ferredoxin IV (FdIV) (Ferredoxin plant-type). Homology to fdxC of R. capsulatus of 62% (FER4_RHOCA). FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. Pfam: 2Fe-2S iron-sulfur clauster binding domain no signal peptide no TMHs; High confidence in function and specificity. | 0.835 |
| azo0524 | fdxD | azo0524 | azo0528 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Ferredoxin V (FdV) (Ferredoxin plant-type). FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. InterPro: Ferredoxin; High confidence in function and specificity. | 0.796 |
| azo0524 | fprA | azo0524 | azo0526 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Probable type A flavoprotein fprA. Homology to frpA of R. capsulatus of 58% (sprot|FPRA_RHOCA) Low-potential electron donor to a number of redox enzymes (Potential). InterPro: Metallo-beta-lactamase superfamily (IPR001279); Flavodoxin (IPR001226) Pfam: Metallo-beta-lactamase superfamily; Flavodoxin no singal peptide no TMHs; Family membership. | 0.563 |
| azo0524 | hoxF | azo0524 | azo1412 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Probable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity. | 0.996 |
| azo0524 | nifQ | azo0524 | azo0529 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Putative NifQ protein. Homology to nifQ of A. vinelandii of 33% (sprot|NIFQ_AZOVI(SRS) NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor (FeMo-co), which is an integral part of the active site of dinitrogenase [2]. The conserved C-terminal cysteine residues may be involved in metal binding. Pfam: NifQ no signal peptide no TMHs; Family membership. | 0.493 |
| azo0524 | nifU | azo0524 | azo0553 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Probable nitrogen fixation protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. | 0.728 |
| azo0524 | nuoA | azo0524 | azo1396 | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | Putative NADH-ubiquinone oxidoreductase chain A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. | 0.973 |
| azo0525 | azo0524 | azo0525 | azo0524 | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | Conserved hypothetical ferredoxin. Homology to fdx of P. stuzeri of 57% (trembl|Q93JV5). Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. InterPro: 4Fe-4S ferredoxin iron-sulfur binding domain (IPR001450) Pfam: 4FE-4S binding domain no signal peptide no TMHs; Family membership. | 0.553 |
| azo0525 | azo0536 | azo0525 | azo0536 | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide. | 0.448 |
| azo0525 | fdxC | azo0525 | azo0527 | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | Ferredoxin IV (FdIV) (Ferredoxin plant-type). Homology to fdxC of R. capsulatus of 62% (FER4_RHOCA). FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. Pfam: 2Fe-2S iron-sulfur clauster binding domain no signal peptide no TMHs; High confidence in function and specificity. | 0.799 |
| azo0525 | fdxD | azo0525 | azo0528 | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | Ferredoxin V (FdV) (Ferredoxin plant-type). FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. InterPro: Ferredoxin; High confidence in function and specificity. | 0.813 |
| azo0525 | fprA | azo0525 | azo0526 | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | Probable type A flavoprotein fprA. Homology to frpA of R. capsulatus of 58% (sprot|FPRA_RHOCA) Low-potential electron donor to a number of redox enzymes (Potential). InterPro: Metallo-beta-lactamase superfamily (IPR001279); Flavodoxin (IPR001226) Pfam: Metallo-beta-lactamase superfamily; Flavodoxin no singal peptide no TMHs; Family membership. | 0.799 |
| azo0525 | nifQ | azo0525 | azo0529 | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | Putative NifQ protein. Homology to nifQ of A. vinelandii of 33% (sprot|NIFQ_AZOVI(SRS) NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor (FeMo-co), which is an integral part of the active site of dinitrogenase [2]. The conserved C-terminal cysteine residues may be involved in metal binding. Pfam: NifQ no signal peptide no TMHs; Family membership. | 0.866 |
| azo0536 | azo0525 | azo0536 | azo0525 | Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide. | Conserved hypothetical protein. Homology to an orf of P. stuzeri of 49% (trembl|Q93JV4). Tigrfam: arsC: arsenate reductase. Pfam: ArsC family (PF03960) no signal peptide. no TMHs. | 0.448 |
| azo0536 | fdxC | azo0536 | azo0527 | Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide. | Ferredoxin IV (FdIV) (Ferredoxin plant-type). Homology to fdxC of R. capsulatus of 62% (FER4_RHOCA). FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. Pfam: 2Fe-2S iron-sulfur clauster binding domain no signal peptide no TMHs; High confidence in function and specificity. | 0.836 |
| azo0536 | fdxD | azo0536 | azo0528 | Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide. | Ferredoxin V (FdV) (Ferredoxin plant-type). FERREDOXINS ARE IRON-SULFUR PROTEINS THAT TRANSFER ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. THIS FERREDOXIN PROBABLY PARTICIPATES IN NITROGEN FIXATION. InterPro: Ferredoxin; High confidence in function and specificity. | 0.768 |
| azo0536 | fprA | azo0536 | azo0526 | Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide. | Probable type A flavoprotein fprA. Homology to frpA of R. capsulatus of 58% (sprot|FPRA_RHOCA) Low-potential electron donor to a number of redox enzymes (Potential). InterPro: Metallo-beta-lactamase superfamily (IPR001279); Flavodoxin (IPR001226) Pfam: Metallo-beta-lactamase superfamily; Flavodoxin no singal peptide no TMHs; Family membership. | 0.558 |
| azo0536 | nifQ | azo0536 | azo0529 | Conserved hypothetical protein. Homology to an orf of Pseudomonas stutzeri of 52% (tremble:Q9EVM9). No domains predicted. No TMHs. No signal peptide. | Putative NifQ protein. Homology to nifQ of A. vinelandii of 33% (sprot|NIFQ_AZOVI(SRS) NifQ is involved in early stages of the biosynthesis of the iron-molybdenum cofactor (FeMo-co), which is an integral part of the active site of dinitrogenase [2]. The conserved C-terminal cysteine residues may be involved in metal binding. Pfam: NifQ no signal peptide no TMHs; Family membership. | 0.775 |