CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.60 | Phosphoenolpyruvate-binding domains |
Domain Context
CATH Clusters
| Superfamily | Phosphoenolpyruvate-binding domains |
| Functional Family | Malyl-CoA lyase |
Enzyme Information
| 4.1.3.24 |
Malyl-CoA lyase.
based on mapping to UniProt Q3J5L6
(1) (S)-malyl-CoA = acetyl-CoA + glyoxylate. (2) (2R,3S)-2-methylmalyl-CoA = propanoyl-CoA + glyoxylate.
-!- The enzymes from Rhodobacter species catalyze a step in the ethylmalonyl-CoA pathway for acetate assimilation. -!- The enzyme from halophilic bacteria participate in the methylaspartate cycle and catalyze the reaction in the direction of malyl-CoA formation. -!- The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25.
|
| 4.1.3.25 |
(S)-citramalyl-CoA lyase.
based on mapping to UniProt Q3J5L6
(3S)-citramalyl-CoA = acetyl-CoA + pyruvate.
-!- The enzyme from the bacterium Clostridium tetanomorphum is a component of EC 4.1.3.22. -!- It also acts on (3S)-citramalyl thioacyl-carrier protein. -!- The enzyme from the bacterium Chloroflexus aurantiacus also has the activity of EC 4.1.3.24. -!- It has no activity with (3R)-citramalyl-CoA (cf. EC 4.1.3.46).
|
UniProtKB Entries (1)
| Q3J5L6 |
MCAL_RHOS4
Rhodobacter sphaeroides 2.4.1
L-malyl-CoA/beta-methylmalyl-CoA lyase
|
PDB Structure
| PDB | 4L9Y |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases.
Bmc Struct.Biol.
|
