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| | ANH92758.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (264 aa) |
| | ANH89729.1 | Hydrogenase expression protein HypE; Derived by automated computational analysis using gene prediction method: Protein Homology. (362 aa) |
| | ANH89730.1 | Hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (599 aa) |
| | ANH89866.1 | Ferredoxin reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (402 aa) |
| | ANH89867.1 | Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (62 aa) |
| | ANH89924.1 | Ferredoxin-1; Derived by automated computational analysis using gene prediction method: Protein Homology. (64 aa) |
| | A8713_01865 | Hypothetical protein; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (118 aa) |
| | ANH90043.1 | Cytochrome C oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (122 aa) |
| | ANH90044.1 | Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (559 aa) |
| | ANH90056.1 | Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (81 aa) |
| | ANH90127.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (123 aa) |
| | ANH95222.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (318 aa) |
| | ANH90206.1 | Hydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (228 aa) |
| | ANH90207.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (490 aa) |
| | ANH90208.1 | NADH-quinone oxidoreductase subunit D; Derived by automated computational analysis using gene prediction method: Protein Homology. (508 aa) |
| | ANH90209.1 | NADH:ubiquinone oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (275 aa) |
| | ANH95223.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (697 aa) |
| | ANH90328.1 | Electron transfer flavoprotein subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology. (320 aa) |
| | ANH93080.1 | Succinate dehydrogenase, cytochrome b556 subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (114 aa) |
| | ANH93267.1 | Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (106 aa) |
| | ANH95656.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (117 aa) |
| | ANH94056.1 | [Fe-S]-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (519 aa) |
| | ANH94580.1 | Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (778 aa) |
| | ANH94884.1 | Ubiquinol-cytochrome c reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (553 aa) |
| | sdhA | Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology. (649 aa) |
| | ANH94653.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (249 aa) |
| | ANH94763.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (596 aa) |
| | ANH94774.1 | Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (72 aa) |
| | ANH90329.1 | Electron transfer flavoprotein subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (262 aa) |
| | ANH90515.1 | Photosystem reaction center subunit H; Derived by automated computational analysis using gene prediction method: Protein Homology. (125 aa) |
| | ANH90740.1 | Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (101 aa) |
| | ANH90987.1 | FeS-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (140 aa) |
| | ANH91027.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa) |
| | A8713_07650 | phosphoribosyl-AMP cyclohydrolase; Incomplete; partial on complete genome; missing stop; Derived by automated computational analysis using gene prediction method: Protein Homology. (211 aa) |
| | ANH91151.1 | Ubiquinol-cytochrome c reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (546 aa) |
| | ANH91152.1 | Ubiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (352 aa) |
| | ANH91153.1 | Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. (269 aa) |
| | ANH91154.1 | Derived by automated computational analysis using gene prediction method: Protein Homology. (206 aa) |
| | ANH91157.1 | Cytochrome C oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (132 aa) |
| | ANH91158.1 | Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (581 aa) |
| | ANH91159.1 | Cytochrome c oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (319 aa) |
| | ANH95336.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (100 aa) |
| | ANH91763.1 | FAD-linked oxidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (468 aa) |
| | ANH92141.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (352 aa) |
| | ANH92374.1 | Cytochrome d ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa) |
| | ANH92375.1 | Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (502 aa) |
| | nuoD | NADH-quinone oxidoreductase subunit 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 a menaquinone. 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. (383 aa) |
| | ANH92725.1 | L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate. (577 aa) |
| | ANH94885.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (130 aa) |
| | ANH94886.1 | Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (571 aa) |
| | ANH95776.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (61 aa) |
| | ANH95000.1 | Photosystem reaction center subunit H; Derived by automated computational analysis using gene prediction method: Protein Homology. (317 aa) |
| | ANH93078.1 | Succinate dehydrogenase flavoprotein subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (584 aa) |
| | ANH93077.1 | Succinate dehydrogenase iron-sulfur subunit; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa) |
| | ANH93033.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (586 aa) |
| | nuoN-2 | 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 a menaquinone. 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. (507 aa) |
| | ANH92887.1 | NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (524 aa) |
| | ANH92886.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (664 aa) |
| | nuoK-2 | 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 a menaquinone. 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. (140 aa) |
| | ANH92884.1 | 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. (226 aa) |
| | ANH92881.1 | Dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (473 aa) |
| | nuoB-2 | Hydroxyacid 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 a menaquinone. 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. (233 aa) |
| | ANH95523.1 | NADH-quinone oxidoreductase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (138 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 a menaquinone. 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. (549 aa) |
| | ANH92857.1 | NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (523 aa) |
| | ANH92856.1 | NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (648 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 a menaquinone. 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. (99 aa) |
| | ANH92854.1 | NADH:ubiquinone oxidoreductase subunit J; 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. (280 aa) |
| | ANH92851.1 | NADH-quinone oxidoreductase subunit G; 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. (834 aa) |
| | ANH92850.1 | NADH oxidoreductase (quinone) subunit F; 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. (458 aa) |
| | ANH92849.1 | NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (289 aa) |
| | nuoD-2 | NADH dehydrogenase subunit 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 a menaquinone. 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. (440 aa) |
| | nuoC | NADH-quinone oxidoreductase subunit C; 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 a menaquinone. 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. (241 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 a menaquinone. 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. (184 aa) |
| | nuoA | NADH-quinone 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 a menaquinone. 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. (119 aa) |
