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EC Tree
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
riboflavin biosynthesis protein,
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aminodioxyphosphoribosylaminopyrimidine reductase
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5-amino-6-(5-phospho-D-ribitylamino)uracil:NADP+ 1'-oxidoreductase
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5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
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5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
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intermediate in the biosynthesis of riboflavin
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5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADPH + H+
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate + NADP+
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5-amino-2,6-dioxy-4-(5'-phosphoribosylamino)pyrimidine + NADPH
5-amino-2,6-dioxy-4-(5'-phosphoribitylamino)pyrimidine + NADP+
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intermediate in the biosynthesis of riboflavin
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NADH
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30% as effective as NADPH
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gene ribD or ribG
UniProt
brenda
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brenda
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additional information
domain structure, overview
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-6°C, 50 mM Tris-HCl, pH 8.0, 1 month
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recombinant enzyme from Escherichia coli to homogeneity
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gene ribD, i.e. ribG, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
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Richter, G.; Fischer, M.; Krieger, C.; Eberhardt, S.; Luttgen, H.; Gerstenschlger, I.; Bacher, A.
Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis
J. Bacteriol.
179
2022-2028
1997
Bacillus subtilis (P17618), Escherichia coli (P25539)
brenda
Burrows, R.B.; Brown, G.M.
Presence in Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin
J. Bacteriol.
136
657-667
1978
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
1.1.1.193 5-amino-6-(5-phosphoribosylamino)uracil reductase
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