EC 3.1.3.104 - 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase

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IntEnz Enzyme Nomenclature
EC 3.1.3.104

Names

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

Reaction

Cofactor

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

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

References

  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 3.1.3.104 created 2016]