Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.104
Description:5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase.
Alternative Name: phosphatase.
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.104
BRENDA Enzyme Link: BRENDA 3.1.3.104
KEGG Enzyme Link: KEGG3.1.3.104
BioCyc Enzyme Link: BioCyc 3.1.3.104
ExPASy Enzyme Link: ExPASy3.1.3.104
EC2PDB Enzyme Link: EC2PDB 3.1.3.104
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.104
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.104
IntEnz Enzyme Link: IntEnz 3.1.3.104
MEDLINE Enzyme Link: MEDLINE 3.1.3.104
MSA:

3.1.3.104;

Phylogenetic Tree:

3.1.3.104;

Uniprot:
M-CSA:
RHEA:25197 5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-(D-ribitylamino)uracil + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases.London N, Farelli JD, Brown SD, Liu C, Huang H, Korczynska M, Al-Obaidi NF, Babbitt PC, Almo SC, Allen KN, Shoichet BK2015 Jan 2025513739
Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis.Haase I, Sarge S, Illarionov B, Laudert D, Hohmann HP, Bacher A, Fischer M2013 Nov 2524123841