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, PDB, CAS registry number:
References:
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. [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. [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. [PMID: 26316208]