CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphoenolpyruvate-binding domains
Functional Family Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase

Enzyme Information

4.1.3.25
(S)-citramalyl-CoA lyase.
based on mapping to UniProt S5N020
(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).
4.1.3.24
Malyl-CoA lyase.
based on mapping to UniProt S5N020
(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.

UniProtKB Entries (1)

S5N020
MCLA_CHLAU
Chloroflexus aurantiacus
Malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase

PDB Structure

PDB 4L7Z
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.
Zarzycki, J., Kerfeld, C.A.
Bmc Struct.Biol.