×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

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 4L80
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.
CATH-Gene3D is a Global Biodata Core Resource Learn more...