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 |
Enzyme Information
| 2.7.1.180 |
FAD:protein FMN transferase.
based on mapping to UniProt O83774
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)
| O83774 |
APBE_TREPA
Treponema pallidum subsp. pallidum str. Nichols
FAD:protein FMN transferase
|
PDB Structure
| PDB | 4XDU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Evidence for Posttranslational Protein Flavinylation in the Syphilis Spirochete Treponema pallidum: Structural and Biochemical Insights from the Catalytic Core of a Periplasmic Flavin-Trafficking Protein.
Mbio
|
