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| Field | Value |
|---|---|
| Gene ID | Lj4g3v0668380 |
| Transcript ID | Lj4g3v0668380.1 |
| Lotus japonicus genome version | MG20 v3.0 |
| Description | Pyruvate kinase [Medicago truncatula] gi|357510595|ref|XP_003625586.1| |
| Working Lj name | n.a. |
Data for domain prediction are obtained with InterProScan, and merged with InterPro data obtained from the EB-eye REST service.
| Prediction algorithm | Identifier | Start | End | Length | E-value | InterPro ID |
|---|---|---|---|---|---|---|
| PANTHER | 7 | 502 | 496 | 0 | – | |
| PANTHER | 7 | 502 | 496 | 0 | ||
| SUPERFAMILY | 9 | 86 | 78 | 1.50E-99 | ||
| CDD | 13 | 502 | 490 | 0 | – | |
| Gene3D | 14 | 83 | 70 | 7.20E-114 | ||
| Pfam | 14 | 356 | 343 | 1.60E-156 | ||
| TIGRFAM | 14 | 493 | 480 | 4.50E-158 | ||
| PRINTS | 70 | 86 | 17 | 1.60E-75 | ||
| SUPERFAMILY | 81 | 180 | 100 | 3.49E-26 | ||
| Gene3D | 84 | 181 | 98 | 1.80E-31 | ||
| SUPERFAMILY | 180 | 354 | 175 | 1.50E-99 | ||
| Gene3D | 182 | 339 | 158 | 7.20E-114 | ||
| PRINTS | 200 | 214 | 15 | 1.60E-75 | ||
| ProSitePatterns | 228 | 240 | 13 | – | ||
| PRINTS | 230 | 256 | 27 | 1.60E-75 | ||
| PRINTS | 257 | 281 | 25 | 1.60E-75 | ||
| PRINTS | 282 | 306 | 25 | 1.60E-75 | ||
| PRINTS | 307 | 325 | 19 | 1.60E-75 | ||
| PRINTS | 326 | 342 | 17 | 1.60E-75 | ||
| SUPERFAMILY | 337 | 502 | 166 | 3.66E-27 | ||
| Gene3D | 340 | 503 | 164 | 4.00E-48 | ||
| Pfam | 373 | 499 | 127 | 5.90E-25 |
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 | Magnesium ion binding | Interacting selectively and non-covalently with magnesium (Mg) ions. | ||
| 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. | ||
| Molecular function | Pyruvate kinase activity | Catalysis of the reaction: ATP + pyruvate = ADP + phosphoenolpyruvate. | ||
| Biological process | Glycolytic process | The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. | ||
| Molecular function | Potassium ion binding | Interacting selectively and non-covalently with potassium (K+) ions. |
Expression pattern of Lj4g3v0668380.1, powered by ExpAt. For advanced configuration, data transformation and export options, view expression data in the ExpAt application.
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A list of the top 25 highly co-expressed genes of Lj4g3v0668380.1, powered by CORGI.
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