Your Input: | |||||
GY26_02270 | Cytochrome c, class I; Derived by automated computational analysis using gene prediction method: Protein Homology. (152 aa) | ||||
GY26_02420 | Copper chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. (154 aa) | ||||
GY26_02425 | Electron transporter SenC; Derived by automated computational analysis using gene prediction method: Protein Homology. (192 aa) | ||||
GY26_06615 | Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (470 aa) | ||||
GY26_06620 | Ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (333 aa) | ||||
GY26_06900 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (432 aa) | ||||
GY26_07525 | Subunit A of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; in S. meliloti it is known to be involved with K+; Derived by automated computational analysis using gene prediction method: Protein Homology. (934 aa) | ||||
GY26_07530 | NADH-ubiquinone oxidoreductase subunit 4L; Derived by automated computational analysis using gene prediction method: Protein Homology. (116 aa) | ||||
GY26_07535 | Cation:proton antiporter; Derived by automated computational analysis using gene prediction method: Protein Homology. (504 aa) | ||||
GY26_07540 | Cation:proton antiporter; Derived by automated computational analysis using gene prediction method: Protein Homology. (165 aa) | ||||
GY26_07545 | Cation:proton antiporter; Derived by automated computational analysis using gene prediction method: Protein Homology. (89 aa) | ||||
GY26_07550 | Sodium:proton antiporter; Derived by automated computational analysis using gene prediction method: Protein Homology. (130 aa) | ||||
GY26_09880 | Cytochrome O ubiquinol oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (309 aa) | ||||
GY26_09885 | Cytochrome o ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (660 aa) | ||||
GY26_09890 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (205 aa) | ||||
GY26_09895 | Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (110 aa) | ||||
cyoE | Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (297 aa) | ||||
GY26_13650 | Cytochrome C oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (115 aa) | ||||
GY26_13655 | Cytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (197 aa) | ||||
GY26_17210 | Acyl carrier protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (88 aa) | ||||
nuoB | 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. (225 aa) | ||||
nuoC | 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. (586 aa) | ||||
GY26_17645 | NADH dehydrogenase; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (167 aa) | ||||
GY26_17650 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (446 aa) | ||||
GY26_17655 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. (927 aa) | ||||
nuoH | 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. (327 aa) | ||||
nuoI | 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. (182 aa) | ||||
GY26_17670 | Hypothetical protein; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (214 aa) | ||||
nuoK | NADH-quinone oxidoreductase subunit K; 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. (102 aa) | ||||
GY26_17680 | NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (621 aa) | ||||
GY26_17685 | NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (508 aa) | ||||
nuoN | 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. (484 aa) | ||||
GY26_17850 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (518 aa) | ||||
GY26_17855 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (181 aa) | ||||
nuoN-2 | NADH-quinone oxidoreductase subunit L; 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. (469 aa) | ||||
GY26_18205 | Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (494 aa) | ||||
GY26_18210 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (628 aa) | ||||
nuoK-2 | 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; Belongs to the complex I subunit 4L family. (101 aa) | ||||
GY26_18220 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (206 aa) | ||||
GY26_18225 | NuoH2 NADH chain H; Derived by automated computational analysis using gene prediction method: Protein Homology. (308 aa) | ||||
GY26_18230 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (293 aa) | ||||
GY26_18240 | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (115 aa) | ||||
GY26_18530 | Alpha/beta hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology. (338 aa) |