Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR018523 is a Isocitrate lyase/phosphorylmutase, conserved site.
<p>Isocitrate lyase ([ec:4.1.3.1]) [[cite:PUB00005064], [cite:PUB00002339]] 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.</p> <p>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.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: isocitrate lyase 2-like [Glycine max] gi|356542840|ref|XP_003539873.1| | 11 | ||
| – | Isocitrate lyase; TAIR: AT3G21720.1 isocitrate lyase; Swiss-Prot: sp|P45457|ACEA2_SOYBN Isocitrate lyase 2; TrEMBL-Plants: tr|I1LRR9|I1LRR9_SOYBN Isocitrate lyase; Found in the gene: LotjaGi3g1v0464400 | 14 | ||
| – | Isocitrate lyase; TAIR: AT3G21720.1 isocitrate lyase; Swiss-Prot: sp|P45457|ACEA2_SOYBN Isocitrate lyase 2; TrEMBL-Plants: tr|I1LRR9|I1LRR9_SOYBN Isocitrate lyase; Found in the gene: LotjaGi3g1v0464400 | 14 | ||
| – | Isocitrate lyase; TAIR: AT3G21720.1 isocitrate lyase; Swiss-Prot: sp|P45457|ACEA2_SOYBN Isocitrate lyase 2; TrEMBL-Plants: tr|I1LRR9|I1LRR9_SOYBN Isocitrate lyase; Found in the gene: LotjaGi3g1v0464400 | 14 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd00377 | CDD | 1 | 25.00 |