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
IPR000887 is a KDPG/KHG aldolase.
<p>4-Hydroxy-2-oxoglutarate aldolase ([ec:4.1.3.16]) (KHG-aldolase) catalyzes the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. Phospho-2-dehydro-3-deoxygluconate aldolase ([ec:4.1.2.14]) (KDPG-aldolase) catalyzes the interconversion of 6-phospho-2-dehydro-3-deoxy-D-gluconate into pyruvate and glyceraldehyde 3-phosphate. E. coli Eda is a KDPG-aldolase that has also been found to have a role in the degradation of 2-keto-4-hydroxyglutarate (KHG) to pyruvate and glyoxylate [[cite:PUB00087307]]. In fact, KHG-aldolase and Eda are the same enzyme [[cite:PUB00087308]].</p> <p>This family consists of KHG/KDPG aldolases, and also includes 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolase. KDPGal-aldolase catalyzes an identical reaction to KDPG, differing in substrate specificity in only the configuration of a single stereocentre [[cite:PUB00049619]].</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 | Lyase activity | Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: KHG/KDPG aldolase-like [Glycine max] gi|356531792|ref|XP_003534460.1| | 8 | ||
| – | PREDICTED: KHG/KDPG aldolase-like [Glycine max] gi|356531792|ref|XP_003534460.1| | 8 | ||
| – | KHG/KDPG aldolase; TAIR: AT4G37590.1 Phototropic-responsive NPH3 family protein; Swiss-Prot: sp|P50846|ALKH_BACSU KHG/KDPG aldolase; TrEMBL-Plants: tr|A0A0S3RS39|A0A0S3RS39_PHAAN Uncharacterized protein; Found in the gene: LotjaGi1g1v0499300 | 14 | ||
| – | KHG/KDPG aldolase; TAIR: AT3G47000.1 Glycosyl hydrolase family protein; Swiss-Prot: sp|P50846|ALKH_BACSU KHG/KDPG aldolase; TrEMBL-Plants: tr|A2Q5T0|A2Q5T0_MEDTR KDPG and KHG aldolase; Found in the gene: LotjaGi1g1v0499300 | 8 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd00452 | CDD | 1 | 25.00 |