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MnmC family methyltransferase
This family is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase. It is often found in association with Pfam:PF01266, where it is responsible for catalysing the transfer of a methyl group from S-adenosyl-L-methionine to 5-aminomethyl-2-thiouridine to form 5-methylaminomethyl-2-thiouridine [1,2]. [1]. 15247431. Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. Bujnicki JM, Oudjama Y, Roovers M, Owczarek S, Caillet J, Droogmans L;. RNA. 2004;10:1236-1242. [2]. 18186482. Sequence-structure-function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA. Roovers M, Oudjama Y, Kaminska KH, Purta E, Caillet J, Droogmans L, Bujnicki JM;. Proteins. 2008;71:2076-2085. (from Pfam)
FAD-dependent oxidoreductase
This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1. [1]. 9153426. Active site plasticity in D-amino acid oxidase: a crystallographic analysis. Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A;. Biochemistry 1997;36:5853-5860. (from Pfam)
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA: the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, and the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34
tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD
This HMM describes either the N-terminal region, called MNMC2, of the tRNA modification bifunctional enzyme MnmC, or a free-standing protein that performs the same methyltransferase function, in partnership with an FAD-dependent protein, or C-terminal region, called MNMC1 (see TIGR03197).
FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC
This HMM represents MnmC1, the FAD-dependent oxidation subunit, or C-terminal region of a bifunctional MnmC, involved in tRNA modification. In Escherichia coli, MnmC (previously known as YfcK) is bifunctional enzyme. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. The N-terminal region, or subunit, contains methyltransferase activity and is known as MnmC2.
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