Your Input: | |||||
AGP52775.1 | FAD-dependent pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (360 aa) | ||||
AGP52872.1 | 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. (554 aa) | ||||
AGP52904.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (435 aa) | ||||
AGP54132.1 | NADH dehydrogenase subunit F; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (612 aa) | ||||
atpC | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (125 aa) | ||||
atpD | ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (472 aa) | ||||
atpG | F0F1 ATP synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (304 aa) | ||||
atpA | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (523 aa) | ||||
atpH | F0F1 ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (271 aa) | ||||
atpF | F0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (187 aa) | ||||
atpE | ATP synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (80 aa) | ||||
atpB | F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (269 aa) | ||||
AGP55249.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (651 aa) | ||||
AGP55250.1 | Catalyzes the fumarate and succinate interconversion; fumarate reductase is used under anaerobic conditions with glucose or glycerol as carbon source; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (256 aa) | ||||
AGP55581.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (193 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 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. (519 aa) | ||||
AGP55903.1 | NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (537 aa) | ||||
AGP55904.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (668 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. (133 aa) | ||||
AGP55906.1 | 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. (201 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. (209 aa) | ||||
nuoH | 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. This subunit may bind ubiquinone. (321 aa) | ||||
nuoB | NADH-quinone oxidoreductase subunit B; 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. (220 aa) | ||||
nuoA | NADH-ubiquinone oxidoreductase subunit 3; 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. (140 aa) | ||||
nuoN-2 | 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. (550 aa) | ||||
AGP55930.1 | NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (554 aa) | ||||
AGP55931.1 | NADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (631 aa) | ||||
nuoK-2 | NADH:ubiquinone 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) | ||||
AGP55933.1 | 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. (307 aa) | ||||
nuoI-2 | (4Fe-4S)-binding 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. (210 aa) | ||||
nuoH-2 | NADH:ubiquinone 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. (452 aa) | ||||
AGP55936.1 | NADH dehydrogenase 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. (460 aa) | ||||
AGP55937.1 | NADH dehydrogenase subunit E; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (276 aa) | ||||
nuoD | 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. (444 aa) | ||||
nuoC | NADH dehydrogenase 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. (247 aa) | ||||
nuoB-2 | NADH dehydrogenase subunit B; 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-2 | NADH dehydrogenase 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) | ||||
AGP56121.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (435 aa) | ||||
AGP56576.1 | Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (544 aa) | ||||
AGP56577.1 | Cytochrome C oxidase assembly protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (333 aa) | ||||
ppa | Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (163 aa) | ||||
nuoD-2 | 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. (380 aa) | ||||
ppk | Polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (714 aa) | ||||
AGP57177.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (257 aa) | ||||
AGP57178.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (584 aa) | ||||
AGP57179.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (156 aa) | ||||
AGP57180.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (114 aa) | ||||
AGP57290.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (441 aa) | ||||
AGP57619.1 | Menaquinol-cytochrome C reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (563 aa) | ||||
AGP57783.1 | 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. (591 aa) | ||||
ppa-2 | Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (169 aa) | ||||
AGP58522.1 | Cytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (320 aa) | ||||
AGP58523.1 | 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. (579 aa) | ||||
AGP58527.1 | Derived by automated computational analysis using gene prediction method: GeneMarkS+. (206 aa) | ||||
AGP58528.1 | Cystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (269 aa) | ||||
AGP58529.1 | Ubiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (351 aa) | ||||
AGP58530.1 | Menaquinol-cytochrome C reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (545 aa) | ||||
ctaB | 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. (306 aa) | ||||
AGP58739.1 | Cytochrome B561; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (330 aa) | ||||
AGP58907.1 | 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. (569 aa) | ||||
AGP59907.1 | Polyphosphate kinase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (309 aa) | ||||
AGP60445.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (248 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: GeneMarkS+. (655 aa) | ||||
AGP60447.1 | Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (240 aa) | ||||
AGP60533.1 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (340 aa) | ||||
AGP60534.1 | Cytochrome BD ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (477 aa) | ||||
AGP61018.1 | Transcriptional regulator; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (293 aa) | ||||
AGP61285.1 | NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: GeneMarkS+. (445 aa) |