Butyryl-CoA dehydrogenase converts the Butanoyl-CoA to 2-butenoyl-CoA. It uses electron transfer flavoprotein (FAD) as its electron acceptor; Localized in the cytoplasm; High confidence in function and specificity.

Acyl-CoA dehydrogenase is involved in fatty acid degradation. It catalyzes the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3- enoyl CoA-products with concommitant reduction of enzyme- bound FAD. In Bacillus subtilis, this protein, formerly known as yusJ protein, has been renamed FadE by Matsuoka et al (JBC, 2007). Localized in the cytoplasm; Specificity unclear.

Acyl-CoA dehydrogenases catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein). These enzymes are homodimers containing one molecule of FAD; Localized in the cytoplasm; Specificity unclear.

Glutaryl-CoA dehydrogenase catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO2 in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism; Uses FAD as prosthetic group; Belongs to the acyl-CoA dehydrogenase family; Localized in the cytoplasm; High confidence in function and specificity.

Glutamate synthase [NADPH] small chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...]

3-Hydroxyl-CoA dehydrogenase / Enoyl-CoA hydratase; Modular protein containing a N-terminal 3-Hydroxyl-CoA dehydrogenase domain and a C-terminal Enoyl-CoA hydratase domain. In Bacillus subtilis, this protein was formerly known as YusL, and has been renamed FadN by Matsuoka et al (JBC, 2007). FadN is involved in fatty acid degradation. 3-Hydroxyl-CoA dehydrogenase catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. It uses NAD as cofactor. Enoyl-CoA hydratase catalyzes the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA. Localized in the cytoplasm; High confidence in [...]

Acyl-coA oxidase, with FAD cofactor, converts acyl-CoA into trans-2-enoyl-CoA; Acts on CoA derivatives of fatty acids with chain length from C(8) to C(18); Family membership.

Succinyl-CoA ligase [ADP-forming] subunit alpha; 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.

Membrane protein that could be the permease component of an ABC transporter (importer); Contains six N-terminal transmembrane segments; Localized in the cytoplasmic membrane; Specificity unclear.