CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1670 | UbiD C-terminal domain-like |
|
3.40.1670.10 | UbiD C-terminal domain-like |
Domain Context
CATH Clusters
| Superfamily | UbiD C-terminal domain-like |
| Functional Family | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase |
Enzyme Information
| 4.1.1.98 |
4-hydroxy-3-polyprenylbenzoate decarboxylase.
based on mapping to UniProt P0AAB5
A 4-hydroxy-3-polyprenylbenzoate = a 2-polyprenylphenol + CO(2).
-!- The enzyme catalyzes a step in prokaryotic ubiquinone biosynthesis, as well as in plastoquinone biosynthesis in cyanobacteria. -!- The enzyme can accept substrates with different polyprenyl tail lengths in vitro, but uses a specific length in vivo, which is determined by the polyprenyl diphosphate synthase that exists in the specific organism. -!- It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129.
|
UniProtKB Entries (1)
| P0AAB5 |
UBID_ECOL6
Escherichia coli CFT073
3-octaprenyl-4-hydroxybenzoate carboxy-lyase
|
PDB Structure
| PDB | 5M1C |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.
J. Biol. Chem.
|
