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Fdx_2 | Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (85 aa) | ||||
PetC | Derived by automated computational analysis using gene prediction method: Protein Homology. (241 aa) | ||||
PetB | Cytochrome b; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (408 aa) | ||||
PetA | Ubiquinol-cytochrome c reductase iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (194 aa) | ||||
OOS06297.1 | Cyclophilin; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (169 aa) | ||||
OOS05733.1 | Nucleoside-diphosphate sugar epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology. (236 aa) | ||||
PtrA | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. (461 aa) | ||||
OOS05510.1 | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. (500 aa) | ||||
OOS05153.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (71 aa) | ||||
YtpA | Lysophospholipase; Derived by automated computational analysis using gene prediction method: Protein Homology. (306 aa) | ||||
nuoB | Hypothetical protein; 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. (223 aa) | ||||
nuoC | NADH-quinone oxidoreductase subunit C/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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. (582 aa) | ||||
NuoE | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (169 aa) | ||||
NuoF | NADH oxidoreductase (quinone) subunit F; Derived by automated computational analysis using gene prediction method: Protein Homology. (478 aa) | ||||
NuoG | NADH-quinone oxidoreductase subunit G; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (1022 aa) | ||||
nuoH | NADH-quinone oxidoreductase subunit 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. (345 aa) | ||||
nuoI | NADH-quinone oxidoreductase subunit I; 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. (182 aa) | ||||
nuoK | NADH-quinone oxidoreductase subunit J; 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 4L family. (110 aa) | ||||
NuoL | NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (623 aa) | ||||
NuoM | NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (534 aa) | ||||
nuoN | NADH-quinone 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. (491 aa) | ||||
Fdx_1 | Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (83 aa) | ||||
OOS02353.1 | (2Fe-2S)-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (105 aa) |