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| Field | Value |
|---|---|
| Gene ID | Lj4g3v2081410 |
| Transcript ID | Lj4g3v2081410.1 |
| Related isoforms 2 | |
| Lotus japonicus genome version | MG20 v3.0 |
| Description | PREDICTED: l-Lysine-8-amino-7-oxononanoate aminotransferase-like [Glycine max] gi|356550752|ref|XP_003543748.1| |
| 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 |
|---|---|---|---|---|---|---|
| SignalP | 1 | 14 | 14 | – | – | |
| Gene3D | 33 | 94 | 62 | 3.60E-54 | ||
| Hamap | 33 | 285 | 253 | 17.044 | ||
| SUPERFAMILY | 35 | 95 | 61 | 7.36E-22 | ||
| Pfam | 36 | 288 | 253 | 9.20E-42 | – | |
| SUPERFAMILY | 131 | 294 | 164 | 7.36E-22 | ||
| Gene3D | 136 | 295 | 160 | 3.60E-54 | ||
| PANTHER | 238 | 298 | 61 | 4.50E-259 | – | |
| PANTHER | 238 | 298 | 61 | 4.50E-259 | ||
| Gene3D | 320 | 384 | 65 | 1.30E-20 | ||
| PANTHER | 321 | 532 | 212 | 4.50E-259 | ||
| PANTHER | 321 | 532 | 212 | 4.50E-259 | – | |
| SUPERFAMILY | 330 | 524 | 195 | 9.30E-64 | ||
| Gene3D | 389 | 541 | 153 | 1.90E-71 | ||
| Pfam | 397 | 809 | 413 | 1.10E-47 | ||
| PANTHER | 560 | 820 | 261 | 4.50E-259 | – | |
| PANTHER | 560 | 820 | 261 | 4.50E-259 | ||
| SUPERFAMILY | 569 | 816 | 248 | 9.30E-64 | ||
| Gene3D | 574 | 711 | 138 | 1.90E-71 | ||
| ProSitePatterns | 623 | 660 | 38 | – | ||
| Gene3D | 718 | 819 | 102 | 1.30E-20 |
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 | Dethiobiotin synthase activity | Catalysis of the reaction: 7,8-diaminononanoate + ATP + CO(2) = ADP + dethiobiotin + 4 H(+) + phosphate. | ||
| Molecular function | ATP binding | Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | ||
| Molecular function | Transaminase activity | Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid. | ||
| Biological process | Biotin biosynthetic process | The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid. | ||
| Molecular function | Pyridoxal phosphate binding | Interacting selectively and non-covalently with pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
Expression pattern of Lj4g3v2081410.1, 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 Lj4g3v2081410.1, powered by CORGI.
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