EC - 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase

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IntEnz Enzyme Nomenclature


Accepted name:
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase
Other name:
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase
Systematic name:
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphohydrolase




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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Haase, I., Sarge, S., Illarionov, B., Laudert, D., Hohmann, H. P., Bacher, A., Fischer, M.
    Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis.
    Chembiochem 14 : 2272-2275 (2013). [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., Shoichet, B. K.
    Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases.
    Biochemistry 54 : 528-537 (2015). [PMID: 25513739]
  3. Sarge, S., Haase, I., Illarionov, B., Laudert, D., Hohmann, H. P., Bacher, A., Fischer, M.
    Catalysis of an Essential Step in Vitamin?B2 Biosynthesis by a Consortium of Broad Spectrum Hydrolases.
    Chembiochem 16 : 2466-2469 (2015). [PMID: 26316208]

[EC created 2016]