| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cysI | cysJ | UGYR_13500 | UGYR_13495 | Sulfite reductase subunit beta; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. | 0.999 |
| cysI | hcr | UGYR_13500 | UGYR_16350 | Sulfite reductase subunit beta; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.823 |
| cysI | ycbX_2 | UGYR_13500 | UGYR_00025 | Sulfite reductase subunit beta; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.886 |
| cysJ | cysI | UGYR_13495 | UGYR_13500 | Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. | Sulfite reductase subunit beta; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.999 |
| cysJ | hcr | UGYR_13495 | UGYR_16350 | Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.901 |
| cysJ | ycbX_2 | UGYR_13495 | UGYR_00025 | Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.977 |
| hcr | cysI | UGYR_16350 | UGYR_13500 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfite reductase subunit beta; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.823 |
| hcr | cysJ | UGYR_16350 | UGYR_13495 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family. | 0.901 |
| hcr | iscS | UGYR_16350 | UGYR_05915 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | 0.847 |
| hcr | ndhC | UGYR_16350 | UGYR_04800 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH:ubiquinone oxidoreductase subunit 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. | 0.852 |
| hcr | nuoB | UGYR_16350 | UGYR_04795 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; 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. | 0.840 |
| hcr | nuoD | UGYR_16350 | UGYR_04790 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH:ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. | 0.975 |
| hcr | nuoH | UGYR_16350 | UGYR_04770 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH:ubiquinone oxidoreductase; 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. | 0.836 |
| hcr | nuoM | UGYR_16350 | UGYR_04745 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.839 |
| hcr | nuoN | UGYR_16350 | UGYR_04740 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH:ubiquinone oxidoreductase subunit N; 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. | 0.840 |
| hcr | ycbX_2 | UGYR_16350 | UGYR_00025 | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.941 |
| iscS | hcr | UGYR_05915 | UGYR_16350 | Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.847 |
| iscS | ycbX_2 | UGYR_05915 | UGYR_00025 | Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.831 |
| ndhC | hcr | UGYR_04800 | UGYR_16350 | NADH:ubiquinone oxidoreductase subunit 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. | HCP oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.852 |
| ndhC | nuoB | UGYR_04800 | UGYR_04795 | NADH:ubiquinone oxidoreductase subunit 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. | NADH dehydrogenase; 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. | 0.999 |