1.14.11.6: thymine dioxygenase
This is an abbreviated version!
For detailed information about thymine dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.6
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1.14.11.6
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pyrimidine
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leishmania
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crassa
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glucosylated
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neurospora
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alpha-ketoglutarate
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ascorbate
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trypanosomes
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deoxyribonucleoside
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glutinis
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rhodotorula
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2'-hydroxylase
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5-hydroxymethylcytosine
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telomeric
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salvage
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kinetoplastids
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deoxyuridine
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protozoa
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alpha-ketoglutarate-dependent
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5-formyluracil
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small-angle
- 1.14.11.6
- pyrimidine
- leishmania
- crassa
-
glucosylated
- neurospora
- alpha-ketoglutarate
- ascorbate
-
trypanosomes
- deoxyribonucleoside
- glutinis
-
rhodotorula
-
2'-hydroxylase
-
5-hydroxymethylcytosine
-
telomeric
-
salvage
- kinetoplastids
- deoxyuridine
-
protozoa
-
alpha-ketoglutarate-dependent
- 5-formyluracil
-
small-angle
Reaction
Synonyms
5-hydroxy-methyluracil dioxygenase, 5-hydroxy-methyluracil oxygenase, EC 1.14.11.5, Fe2+/2-oxoglutarate dependent hydroxylase, J binding protein 1, J binding protein 2, J-binding protein 1, J-binding protein 2, JBP1, JBP2, More, T7H, thymidine hydroxylase, thymine 7-hydroxylase, thymine dioxygenase, thymine hydroxylase, thymine-7-hydroxylase
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Metals Ions
Metals Ions on EC 1.14.11.6 - thymine dioxygenase
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Fe2+
additional information
Fe2+
4 residues within this motif are critical for the coordination of Fe2+ and 2-oxoglutarate binding as well as functionality of this family of enzymes
Fe2+
acts as cofactor, 4 residues within this motif are critical for the coordination of Fe2+ and 2-oxoglutarate binding as well as functionality of this family of enzymes
Ni2+ and Ca2+ cannot substitute for Fe2+, binding structure with truncated enzyme mutant. Residues His214, Asp216 and His271 play essential roles in the metal ion binding
additional information
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Ni2+ and Ca2+ cannot substitute for Fe2+, binding structure with truncated enzyme mutant. Residues His214, Asp216 and His271 play essential roles in the metal ion binding