| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| fdh1B | fdxB | azo3039 | azo0556 | 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. | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | 0.996 |
| fdh1B | hoxF | azo3039 | azo1412 | 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. | 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. | 0.998 |
| fdh1B | nuoA | azo3039 | azo1396 | 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. | 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. | 0.998 |
| fdh1B | nuoC | azo3039 | azo1398 | 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. | Respiratory-chain NADH dehydrogenase, chain C probable; 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 30 kDa subunit family. | 0.998 |
| fdh1B | nuoD | azo3039 | azo1399 | 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. | Putative NADH-ubiquinone oxidoreductase chain D; 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 49 kDa subunit family. | 0.998 |
| fdh1B | nuoH | azo3039 | azo1403 | 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. | Putative NADH-ubiquinone oxidoreductase chain H; 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. This subunit may bind ubiquinone. | 0.998 |
| fdh1B | nuoM | azo3039 | azo1408 | 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. | Putative NADH-ubiquinone oxidoreductase, chain M; NADH-quinone oxidoreductase chain M (EC 1.6.99.5) (NADH dehydrogenase I chain M) (NDH-1 chain M). 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. InterPro: NADH-Ubiquino [...] | 0.998 |
| fdh1B | nuoN | azo3039 | azo1409 | 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. | NADH-ubiquinone oxidoreductase, chain N probable; 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 2 family. | 0.998 |
| fdxB | fdh1B | azo0556 | azo3039 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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 |
| fdxB | hoxF | azo0556 | azo1412 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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 |
| fdxB | nifD | azo0556 | azo0539 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | Nitrogenase molybdenum-iron protein alpha chain (EC 1.18.6.1) (Nitrogenase component I) (Dinitrogenase). The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex which has 2 components: the iron protein and the molybdenum-iron protein; High confidence in function and specificity. | 0.965 |
| fdxB | nifK | azo0556 | azo0540 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | Nitrogenase molybdenum-iron protein beta chain; This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation; Belongs to the NifD/NifK/NifE/NifN family. | 0.968 |
| fdxB | nuoA | azo0556 | azo1396 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | 0.974 |
| fdxB | nuoC | azo0556 | azo1398 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | Respiratory-chain NADH dehydrogenase, chain C probable; 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 30 kDa subunit family. | 0.976 |
| fdxB | nuoD | azo0556 | azo1399 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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 D; 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 49 kDa subunit family. | 0.976 |
| fdxB | nuoH | azo0556 | azo1403 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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 H; 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. This subunit may bind ubiquinone. | 0.974 |
| fdxB | nuoM | azo0556 | azo1408 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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 M; NADH-quinone oxidoreductase chain M (EC 1.6.99.5) (NADH dehydrogenase I chain M) (NDH-1 chain M). 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. InterPro: NADH-Ubiquino [...] | 0.974 |
| fdxB | nuoN | azo0556 | azo1409 | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | NADH-ubiquinone oxidoreductase, chain N probable; 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 2 family. | 0.973 |
| hoxF | fdh1B | azo1412 | azo3039 | 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. | 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. | 0.998 |
| hoxF | fdxB | azo1412 | azo0556 | 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. | Probable ferredoxin. Homology to fdxB of R. capsulatus of 45% (sprot|FER3_RHOCA) 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. | 0.996 |