Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.49
Description:Uridine-5'-phosphate dioxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.49
BRENDA Enzyme Link: BRENDA 1.14.11.49
KEGG Enzyme Link: KEGG1.14.11.49
BioCyc Enzyme Link: BioCyc 1.14.11.49
ExPASy Enzyme Link: ExPASy1.14.11.49
EC2PDB Enzyme Link: EC2PDB 1.14.11.49
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.49
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.49
IntEnz Enzyme Link: IntEnz 1.14.11.49
MEDLINE Enzyme Link: MEDLINE 1.14.11.49
MSA:

1.14.11.49;

Phylogenetic Tree:

1.14.11.49;

Uniprot:
M-CSA:
RHEA:46500 2-oxoglutarate + O2 + UMP = CO2 + phosphate + succinate + uridine-5'-aldehyde
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[*:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[CH2;+0:12]-[CH;+0:13]1-[*:14]-[*:15]-[CH;+0:16](-[*:17])-[O;H0;+0:18]-1.[O;H0;+0:19]=[O;H0;+0:20]>>[*:17]-[CH;+0:16]1-[*:15]-[*:14]-[CH;+0:13](-[CH;+0:12]=[O;H0;+0:11])-[O;H0;+0:19]-1.[*:5]=[C;H0;+0:4](-[*:6])-[OH;+0:20].[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:18]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Fe(II)-dependent, uridine-5'-monophosphate α-ketoglutarate dioxygenases in the synthesis of 5'-modified nucleosides.Yang Z, Unrine J, Nonaka K, Van Lanen SG201223034228
Characterization of LipL as a non-heme, Fe(II)-dependent α-ketoglutarate:UMP dioxygenase that generates uridine-5'-aldehyde during A-90289 biosynthesis.Yang Z, Chi X, Funabashi M, Baba S, Nonaka K, Pahari P, Unrine J, Jacobsen JM, Elliott GI, Rohr J, Van Lanen SG2011 Mar 1121216959