NCU06296 is a predicted flavin-containing monooxygenase with an FMO-like dinucleotide-binding architecture. Family evidence supports FAD-dependent oxygenation using a reduced nicotinamide cofactor, commonly NADPH. Its physiological substrate, reaction specificity, pathway, and cellular compartment in Neurospora crassa remain unknown.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004497 monooxygenase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The FMO-like catalytic architecture and conserved monooxygenase IBA support broad flavin-dependent oxygenation. Experimentally characterized fungal FMO establishes NADPH/O2-dependent oxidation, while the substrate remains unresolved for this target. Supporting Evidence: file:NEUCR/NCU06296/NCU06296-uniprot.txt DR InterPro; IPR020946; Flavin_mOase-like. PMID:10077572 The flavin-containing monooxygenase from yeast (yFMO) catalyzes the O2- and NADPH-dependent oxidations of biological thiols, including oxidation of glutathione to glutathione disulfide (GSSG). |
| GO:0004499 N,N-dimethylaniline monooxygenase activity | IEA GO_REF:0000002 | UNDECIDED | Summary: IPR020946 identifies a flavin-monooxygenase-like family with diverse substrates; it does not uniquely identify N,N-dimethylaniline as the acceptor. The target lacks retrieved substrate assays or a resolved characterized substrate-specific subfamily, so this exact reaction cannot be confirmed or refuted. Supporting Evidence: file:NEUCR/NCU06296/NCU06296-uniprot.txt DR InterPro; IPR020946; Flavin_mOase-like. PMID:10077572 The flavin-containing monooxygenase from yeast (yFMO) catalyzes the O2- and NADPH-dependent oxidations of biological thiols, including oxidation of glutathione to glutathione disulfide (GSSG). |
| GO:0050660 flavin adenine dinucleotide binding | IEA GO_REF:0000002 | ACCEPT | Summary: FAD is the prosthetic flavin used by the supported FMO catalytic architecture. Family placement supports this cofactor-binding annotation without resolving the oxidized substrate. Supporting Evidence: file:NEUCR/NCU06296/NCU06296-uniprot.txt DR InterPro; IPR020946; Flavin_mOase-like. PMID:10077572 The flavin-containing monooxygenase from yeast (yFMO) catalyzes the O2- and NADPH-dependent oxidations of biological thiols, including oxidation of glutathione to glutathione disulfide (GSSG). |
| GO:0050661 NADP binding | IEA GO_REF:0000002 | ACCEPT | Summary: The FMO dinucleotide-binding architecture and experimentally characterized NADPH-dependent fungal FMO chemistry support conserved NADP(H) cofactor binding. Supporting Evidence: file:NEUCR/NCU06296/NCU06296-uniprot.txt DR InterPro; IPR020946; Flavin_mOase-like. PMID:10077572 The flavin-containing monooxygenase from yeast (yFMO) catalyzes the O2- and NADPH-dependent oxidations of biological thiols, including oxidation of glutathione to glutathione disulfide (GSSG). |
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