Fumarate reductase, anaerobic, membrane anchor polypeptide; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.

Fumarate reductase, anaerobic, flavoprotein subunit; Residues 1 to 602 of 602 are 99.83 pct identical to residues 1 to 602 of 602 from Escherichia coli K-12 Strain MG1655: B4154.

Succinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Succinate dehydrogenase, cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). Belongs to the cytochrome b560 family.

Succinate dehydrogenase, hydrophobic subunit; Membrane-anchoring subunit of succinate dehydrogenase (SDH).

succinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.

succinyl-CoA synthetase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.

Putative oxidoreductase, Fe-S subunit; Residues 1 to 1174 of 1174 are 99.57 pct identical to residues 1 to 1174 of 1174 from Escherichia coli K-12 Strain MG1655: B1378.

NADH dehydrogenase I chain 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 N-terminal section; belongs to the complex I 30 kDa subunit family.