CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphoenolpyruvate-binding domains
Functional Family Isocitrate lyase

Enzyme Information

4.1.3.30
Methylisocitrate lyase.
based on mapping to UniProt P28298
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.
-!- Acts on threo-D(s)-2-methylisocitrate, but not on threo-D(s)- isocitrate, threo-DL-isocitrate or erythro-L(s)-isocitrate.
4.1.3.1
Isocitrate lyase.
based on mapping to UniProt P28298
Isocitrate = succinate + glyoxylate.
-!- The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3- tricarboxylate.

UniProtKB Entries (1)

P28298
ACEA_EMENI
Aspergillus nidulans FGSC A4
Isocitrate lyase

PDB Structure

PDB 1DQU
External Links
Method X-RAY DIFFRACTION
Organism Emericella
Primary Citation
The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans.
Britton, K., Langridge, S., Baker, P.J., Weeradechapon, K., Sedelnikova, S.E., De Lucas, J.R., Rice, D.W., Turner, G.
Structure Fold.Des.