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| FMO5 | Dimethylaniline monooxygenase [N-oxide-forming]. (533 aa) | ||||
| FMO2 | Dimethylaniline monooxygenase [N-oxide-forming]. (532 aa) | ||||
| DPYD | Dihydropyrimidine dehydrogenase [NADP(+)]; Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. (1025 aa) | ||||
| IL4I1 | Interleukin 4 induced 1. (578 aa) | ||||
| FMO3 | Dimethylaniline monooxygenase [N-oxide-forming] 3; Essential hepatic enzyme that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds. Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite. TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thr [...] (532 aa) | ||||
| LOC517828 | Dimethylaniline monooxygenase [N-oxide-forming]. (532 aa) | ||||
| FMO1 | Flavin-containing monooxygenase. (612 aa) | ||||
| FDXR | NADPH:adrenodoxin oxidoreductase, mitochondrial; Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C- 27 hydroxylation in the liver; Belongs to the ferredoxin--NADP reductase type 1 family. (492 aa) | ||||
| PYROXD1 | Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1; Probable FAD-dependent oxidoreductase; involved in the cellular oxidative stress response (By similarity). Required for normal sarcomere structure and muscle fiber integrity (By similarity). (518 aa) | ||||
| FMO4 | Dimethylaniline monooxygenase [N-oxide-forming]. (550 aa) | ||||
| SQOR | Pyr_redox_2 domain-containing protein. (450 aa) | ||||