Conserved Site

Isocitrate lyase/phosphorylmutase, conserved site (IPR018523)

Short name: Isocitrate_lyase_ph_CS

Description

Isocitrate lyase (EC:4.1.3.1) [PMID: 2696959, PMID: 2361956] is an enzyme that catalyzes the conversion of isocitrate to succinate and glyoxylate. This is the first step in the glyoxylate bypass, an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. A cysteine, a histidine and a glutamate or aspartate have been found to be important for the enzyme's catalytic activity. Only one cysteine residue is conserved between the sequences of the fungal, plant and bacterial enzymes; it is located in the middle of a conserved hexapeptide.

Other enzymes also belong to this family including carboxyvinyl-carboxyphosphonate phosphorylmutase (EC:2.7.8.23) which catalyses the conversion of 1-carboxyvinyl carboxyphosphonate to 3-(hydrohydroxyphosphoryl) pyruvate carbon dioxide, and phosphoenolpyruvate mutase (EC:5.4.2.9), which is involved in the biosynthesis of phosphinothricin tripeptide antiobiotics.

GO terms

Biological Process

GO:0008152 metabolic process

Molecular Function

GO:0003824 catalytic activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns