P17606
Gene name |
|
Protein name |
Malate dehydrogenase [NADP] 1, chloroplastic |
Names |
NADP-MDH-1 |
Species |
Sorghum bicolor (Sorghum) (Sorghum vulgare) |
KEGG Pathway |
sbi:8057802 |
EC number |
1.1.1.82: With NAD(+) or NADP(+) as acceptor |
Protein Class |
MALATE DEHYDROGENASE (PTHR23382) |
Descriptions
The chloroplastic NADP-dependent malate dehydrogenase (NADP-MDH) catalyzes the reduction of oxaloacetate into L-malate. The enzyme exhibits extensions at both the N- and C-termini. The N-terminal disulfide motif is inserted in a cleft between the two subunits of the dimer, thereby locking the domains in each subunit. The C-terminal extension (C-terminal inhibitory peptide) also contains a regulatory disulfide bridge. The C-terminal disulfide keeps the C-terminal residues tight to the enzyme surface and blocks access to the active site. Reduction of the N-terminal disulfide may release the stopper between the domains and give the enzyme the flexibility. Simultaneous reduction of the C-terminal disulfide may free the C-terminal residues from binding to the enzyme and make the active site accessible.
Autoinhibitory domains (AIDs)
Target domain |
81-409 (MDH domain) |
Relief mechanism |
Others |
Assay |
Structural analysis, Mutagenesis experiment |
Target domain |
81-409 (MDH domain) |
Relief mechanism |
Others |
Assay |
Structural analysis, Deletion assay |
Accessory elements
No accessory elements
References
- Johansson K et al. (1999) "Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form", Biochemistry, 38, 4319-26
- Krimm I et al. (1999) "Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition", The Journal of biological chemistry, 274, 34539-42
Autoinhibited structure
Activated structure
2 structures for P17606
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 7MDH | X-ray | 240 A | A/B/C/D | 55-429 | PDB |
| AF-P17606-F1 | Predicted | AlphaFoldDB |
No variants for P17606
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P17606 | |||||
No associated diseases with P17606
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.82 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR23382 | MALATE DEHYDROGENASE |
| PANTHER Subfamily | PTHR23382:SF0 | MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED |
| PANTHER Protein Class |
dehydrogenase
oxidoreductase |
|
| PANTHER Pathway Category |
Pyruvate metabolism Lactate Dehydrogenase TCA cycle Malate Dehydrogenase |
|
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| malate dehydrogenase (NADP+) activity | Catalysis of the reaction: (S)-malate + NADP+ = oxaloacetate + NADPH + H+. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| malate metabolic process | The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGLSTAYSPV | GSHLAPAPLG | HRRSAQLHRP | RRALLATVRC | SVDAAKQVQD | GVATAEAPAT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RKDCFGVFCT | TYDLKAEDKT | KSWKKLVNIA | VSGAAGMISN | HLLFKLASGE | VFGQDQPIAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLLGSERSFQ | ALEGVAMELE | DSLYPLLREV | SIGIDPYEVF | EDVDWALLIG | AKPRGPGMER |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AALLDINGQI | FADQGKALNA | VASKNVKVLV | VGNPCNTNAL | ICLKNAPDIP | AKNFHALTRL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DENRAKCQLA | LKAGVFYDKV | SNVTIWGNHS | TTQVPDFLNA | KIDGRPVKEV | IKDTKWLEEE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FTITVQKRGG | ALIQKWGRSS | AASTAVSIAD | AIKSLVTPTP | EGDWFSTGVY | TTGNPYGIAE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DIVFSMPCRS | KGDGDYELAT | DVSMDDFLWE | RIKKSEAELL | AEKKCVAHLT | GEGNAYCDVP |
| EDTMLPGEV |