The Enzyme Database

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Accepted name: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase
Reaction: 5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-(D-ribitylamino)uracil + phosphate
Other name(s): 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate phosphatase
Systematic name: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphohydrolase
Comments: Requires Mg2+. The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis. Most forms of the enzyme has a broad substrate specificity [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Haase, I., Sarge, S., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis. ChemBioChem 14 (2013) 2272–2275. [DOI] [PMID: 24123841]
2.  London, N., Farelli, J.D., Brown, S.D., Liu, C., Huang, H., Korczynska, M., Al-Obaidi, N.F., Babbitt, P.C., Almo, S.C., Allen, K.N. and Shoichet, B.K. Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases. Biochemistry 54 (2015) 528–537. [DOI] [PMID: 25513739]
3.  Sarge, S., Haase, I., Illarionov, B., Laudert, D., Hohmann, H.P., Bacher, A. and Fischer, M. Catalysis of an essential step in vitamin B2 biosynthesis by a consortium of broad spectrum hydrolases. ChemBioChem 16 (2015) 2466–2469. [DOI] [PMID: 26316208]
[EC created 2016]

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