CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.465 | Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 | |
3.30.465.10 |
Domain Context
CATH Clusters
Superfamily | 3.30.465.10 |
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.
Acta Crystallogr.,Sect.D
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