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NAD(P)-binding domain-containing protein
SidA/IucD/PvdA family monooxygenase
This is a family of Rossmann fold oxidoreductases that catalyse NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyses the hydroxylation of L-ornithine at the N5 position [1,2], and L-lysine 6-monooxygenase, which catalyses the hydroxylation of lysine at the N6 position (EC:1.14.13.59) [3]. [1]. 8106324. Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa. Visca P, Ciervo A, Orsi N;. J Bacteriol. 1994;176:1128-1140. [2]. 16233371. dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis. Yamada O, Na Nan S, Akao T, Tominaga M, Watanabe H, Satoh T, Enei H, Akita O;. J Biosci Bioeng. 2003;95:82-88. [3]. 16461464. A genetic locus required for iron acquisition in Mycobacterium tuberculosis. Krithika R, Marathe U, Saxena P, Ansari MZ, Mohanty D, Gokhale RS;. Proc Natl Acad Sci U S A. 2006;103:2069-2074. (from Pfam)
FAD-dependent oxidoreductase
This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)
Flavin-binding monooxygenase-like
This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases. [1]. 9538688. A hydrophobic sequence motif common to N-hydroxylating enzymes. Stehr M, Diekmann H, Smau L, Seth O, Ghisla S, Singh M, Macheroux P;. Trends Biochem Sci 1998;23:56-57. (from Pfam)
flavin-containing monooxygenase
flavin-containing monooxygenase (FMO) catalyses the flavin-dependent oxidation of ketones and cyclic ketones to esters and lactones, by using molecular oxygen and NAD(P)H.
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