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:1.14.11.6
Description:Thymine dioxygenase.
Alternative Name: Thymine,2-oxoglutarate dioxygenase.
Thymine 7-hydroxylase.
Cath: 1.20.120.1440;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.6
BRENDA Enzyme Link: BRENDA 1.14.11.6
KEGG Enzyme Link: KEGG1.14.11.6
BioCyc Enzyme Link: BioCyc 1.14.11.6
ExPASy Enzyme Link: ExPASy1.14.11.6
EC2PDB Enzyme Link: EC2PDB 1.14.11.6
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.6
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.6
IntEnz Enzyme Link: IntEnz 1.14.11.6
MEDLINE Enzyme Link: MEDLINE 1.14.11.6
MSA:

1.14.11.6;

Phylogenetic Tree:

1.14.11.6;

Uniprot:
M-CSA:
RHEA:10316 2-oxoglutarate + O2 + thymine = 5-hydroxymethyluracil + CO2 + succinate
RULE(radius=1) [*:1]-[CH3;+0:2].[*:3]=[C;H0;+0:4](-[OH;+0:5])-[C;H0;+0:6](=[*:7])-[*:8].[O;H0;+0:9]=[O;H0;+0:10]>>[*:1]-[CH2;+0:2]-[OH;+0:9].[*:7]=[C;H0;+0:6](-[*:8])-[OH;+0:10].[*:3]=[C;H0;+0:4]=[O;H0;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Markedly different ascorbate dependencies of the sequential alpha-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis.Warn-Cramer BJ, Macrander LA, Abbott MT1983 Sep 106684117
Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase.Liu CK, Hsu CA, Abbott MT1973 Nov4274083
Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa.Bankel L, Holme E, Lindstedt G, Lindstedt S1972 Mar 1511946494