Sulfur Containing Compound Database
| Gene name | IMDH1 |
| AGI ID | AT5G14200 |
| Gene length | 409 |
| Uniprot ID | Q9FMT1 |
| Protein Name | 3-isopropylmalate dehydrogenase 3 chloroplastic |
| Synonym | IMD1 |
| EC number | EC 1.1.1.85 |
| Entrez Gene | 831270 |
| Refseq mrna | NM_121424 |
| Refseq protein | NP_196924 |
| Function | Knocking out either of the candidate genes; AtleuC1 (IIL1) or AtIMD1 (IMD1) would reduced the level of Met-GSLs indicating that both genes are actually involved in Met-GSL biosynthesis (Sawada & Kuwahara et al. 2009) |
| Group | GSL side chain elongation |
| Reference | He et al. (2011); He et al. (2009); Sawada & Kuwahara et al. (2009) |
| Organism | AGI ID | Gene Name | Protein Name | Identity | E-Value | Description |
|---|---|---|---|---|---|---|
|
Cabbage |
IMDH1 |
3-isopropylmalate dehydrogenase 3 chloroplastic |
91 |
0.00E+00 |
||
|
Cabbage |
IMDH1 |
3-isopropylmalate dehydrogenase 3 chloroplastic |
63 |
3.00E-180 |
||
|
Cabbage |
IMDH1 |
3-isopropylmalate dehydrogenase 3 chloroplastic |
59 |
9.00E-172 |
||
|
Papaya |
IMDH1 |
3-isopropylmalate dehydrogenase 3 chloroplastic |
63 |
1.00E-170 |
||
|
Broccoli |
IMDH1 |
3-isopropylmalate dehydrogenase 3 chloroplastic |
31 |
1.00E-43 |
| GO ID | Ontology | GO Term | Description |
|---|---|---|---|
|
MF |
magnesium ion binding |
Interacting selectively and non-covalently with magnesium (Mg) ions. |
|
|
MF |
3-isopropylmalate dehydrogenase activity |
Catalysis of the reaction: 3-carboxy-2-hydroxy-4-methylpentanoate + NAD+ = 3-carboxy-4-methyl-2-oxopentanoate + NADH + H+. |
|
|
CC |
cytoplasm |
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
|
|
BP |
leucine biosynthetic process |
The chemical reactions and pathways resulting in the formation of leucine, 2-amino-4-methylpentanoic acid. |
|
|
CC |
chloroplast |
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
|
|
CC |
plastid |
Any member of a family of organelles found in the cytoplasm of plants and some protists, which are membrane-bounded and contain DNA. Plant plastids develop from a common type, the proplastid. |
|
|
CC |
chloroplast stroma |
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis. |
|
|
BP |
response to salt stress |
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of salt (parti |
|
|
MF |
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP. |
|
|
BP |
glucosinolate biosynthetic process |
The chemical reactions and pathways resulting in the formation of glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae. |
|
|
MF |
NAD binding |
Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
|
|
BP |
oxidation-reduction process |
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Pubmed ID | Authors | Year | Title | Journal | Description |
|---|---|---|---|---|---|
|
He, Y., Mawhinney, T.P., Preuss, M.L., Schroeder, A.C., Chen, B., Abraham, L., Jez, J.M. & Chen, S. |
2009 |
A redox-active isopropylmalate dehydrogenase functions in the biosynthesis of glucosinolates and leucine in Arabidopsis |
Plant Journal |
||
|
He, Y., Galant, A., Pang, Q., Strul, J.M., Balogun, S.F., Jez, J.M. & Chen, S. |
2011 |
Structural and functional evolution of isopropylmalate dehydrogenases in the leucine and glucosinolate pathways of Arabidopsis thaliana |
J Biol Chem |
||
|
Sawada, Y., Kuwahara, A., Nagano, M., Narisawa, T., Sakata, A., Saito, K. & Yokota Hirai, M. |
2009 |
Omics-based approaches to methionine side chain elongation in Arabidopsis: characterization of the genes encoding methylthioalkylmalate isomerase and methylthioalkylmalate dehydrogenase |
Plant Cell Physiol |