CATH Classification

Domain Context

CATH Clusters

Superfamily FAD/NAD(P)-binding domain
Functional Family

Enzyme Information

1.14.13.234
12-dehydrotetracycline 5-monooxygenase.
based on mapping to UniProt L8EUQ6
12-dehydrotetracycline + NADPH + O(2) = 5a,11a-dehydrooxytetracycline + NADP(+) + H(2)O.
-!- The enzyme, characterized from the bacterium Streptomyces rimosus, is bifunctional, catalyzing two successive monooxygenation reactions. -!- It starts by catalyzing the stereospecific hydroxylation of anhydrotetracycline at C(6) (EC 1.14.13.38). -!- If the released product is captured by EC 1.3.98.4 it is reduced to tetracycline. -!- However, if the released product is recaptured by OxyS, it performs an additional hydroxylation at C(5), producing 5a,11a- dehydrooxytetracycline, which, following the action of EC 1.3.98.4, becomes oxytetracycline.
1.14.13.38
Anhydrotetracycline 6-monooxygenase.
based on mapping to UniProt L8EUQ6
Anhydrotetracycline + NADPH + O(2) = 12-dehydrotetracycline + NADP(+) + H(2)O.
-!- The enzyme, characterized from the bacterium Streptomyces rimosus, participates in the biosynthesis of tetracycline antibiotics. -!- It can also catalyze EC 1.14.13.234.

UniProtKB Entries (1)

L8EUQ6
OXYS_STRR1
Streptomyces rimosus subsp. rimosus ATCC 10970
12-dehydrotetracycline 5-monooxygenase/anhydrotetracycline 6-monooxygenase

PDB Structure

PDB 4K2X
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Uncovering the Enzymes that Catalyze the Final Steps in Oxytetracycline Biosynthesis.
Wang, P., Bashiri, G., Gao, X., Sawaya, M.R., Tang, Y.
J.Am.Chem.Soc.