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CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.462.20
Functional Family

Enzyme Information

1.3.3.14
Aclacinomycin-A oxidase.
based on mapping to UniProt Q0PCD7
Aclacinomycin A + O(2) = aclacinomycin Y + H(2)O(2).
-!- This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. -!- The enzyme utilizes the same active site to catalyze the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A (cf. EC 1.1.3.45) and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y.
1.1.3.45
Aclacinomycin-N oxidase.
based on mapping to UniProt Q0PCD7
Aclacinomycin N + O(2) = aclacinomycin A + H(2)O(2).
-!- This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. -!- The enzyme utilizes the same active site to catalyze the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14).

UniProtKB Entries (1)

Q0PCD7
AKNOX_STRGJ
Streptomyces galilaeus
Aclacinomycin-N/aclacinomycin-A oxidase

PDB Structure

PDB 2IPI
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning.
Sultana, A., Alexeev, I., Kursula, I., Mantsala, P., Niemi, J., Schneider, G.
Acta Crystallogr.,Sect.D
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