CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.10 | Roll | |
3.10.520 | T-fold | |
3.10.520.10 | ApbE-like domains |
Domain Context
CATH Clusters
Superfamily | ApbE-like domains |
Functional Family | FAD:protein FMN transferase |
Enzyme Information
2.7.1.180 |
FAD:protein FMN transferase.
based on mapping to UniProt A5F5Y3
FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP.
-!- The enzyme catalyzes the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1.
|
UniProtKB Entries (1)
A5F5Y3 |
APBE_VIBC3
Vibrio cholerae O395
FAD:protein FMN transferase
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PDB Structure
PDB | 6NXJ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Conserved residue His-257 ofVibrio choleraeflavin transferase ApbE plays a critical role in substrate binding and catalysis.
J.Biol.Chem.
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