Reviewed,
UniProtKB/Swiss-Prot P52426 (MDHP_SPIOL)
Last modified
November 25, 2008.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Malate dehydrogenase [NADP], chloroplastic EC=1.1.1.82 Alternative name(s): NADP-MDH | ||
| Gene names |
| ||
| Organism | Spinacia oleracea (Spinach) | ||
| Taxonomic identifier | 3562 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia |
Protein attributes
| Sequence length | 435 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells. |
| Catalytic activity | (S)-malate + NADP(+) = oxaloacetate + NADPH. |
| Enzyme regulation | Chloroplast NADP-MDH is activated upon illumination. In order to be enzymatically active, disulfides bridges on the protein must be reduced by thioredoxin which receives electrons from ferredoxin and the electron transport system of photosynthesis By similarity. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Domain | Removal of amino acids 57 to 76 results in the formation of active monomers, a shift of the pH optimum from 8 to 7, the loss of oxaloacetate inhibition and an increased maximal velocity. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 2 family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 45 | 45 | Chloroplast | ||||||||
| Chain | 46 – 435 | 390 | Malate dehydrogenase [NADP], chloroplastic | PRO_0000018649 | |||||||
Regions | |||||||||||
| Nucleotide binding | 98 – 104 | 7 | NADP By similarity | ||||||||
| Nucleotide binding | 216 – 218 | 3 | NADP By similarity | ||||||||
Sites | |||||||||||
| Active site | 274 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 179 | 1 | Substrate By similarity | ||||||||
| Binding site | 185 | 1 | Substrate By similarity | ||||||||
| Binding site | 192 | 1 | NADP By similarity | ||||||||
| Binding site | 199 | 1 | NAD By similarity | ||||||||
| Binding site | 218 | 1 | Substrate By similarity | ||||||||
| Binding site | 249 | 1 | Substrate By similarity | ||||||||
| Site | 69 | 1 | Activation of NADP-MDH By similarity | ||||||||
| Site | 74 | 1 | Activation of NADP-MDH By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 69 ↔ 74 | In oxidized inactive NAD-MDH By similarity | |||||||||
| Disulfide bond | 410 ↔ 422 | In oxidized inactive NAD-MDH By similarity | |||||||||
Sequences
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References
| [1] | "Full-length cDNA sequence for chloroplast NADP-dependent malate dehydrogenase from spinach (Spinacia oleracea L.)." Harnecker J., Scheibe R., von Schaewen A. (er) Plant Gene Register PGR95-106 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf mesophyll. |
| [2] | "Effects of N-terminal truncations upon chloroplast NADP-malate dehydrogenases from pea and spinach." Ocheretina O., Harnecker J., Rother T., Schmid R., Scheibe R. Biochim. Biophys. Acta 1163:10-16(1993) [PubMed: 8476924] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-84, MUTAGENESIS. |
Cross-references
Sequence databases | |
|---|---|
| X84020 mRNA. Translation: CAA58848.1. | |
| PIR | S52268. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CIV based on UniProtKB P46489. |
| SMR | P52426. Positions 66-432. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR001236. Lactate/malate_DHase. IPR015955. Lactate_DHase/Glyco_Ohase_4_C. IPR001252. Malate_DHase_AS. IPR011273. Malate_DHase_NADP-dep_pln. IPR010945. Malate_DHase_SF1. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR23382. MDH_SF1. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| ProDom | PD003052. Mal_dehydrog. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01757. Malate-DH_plant. 1 hit. TIGR01759. MalateDH-SF1. 1 hit. |
| PROSITE | PS00068. MDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MDHP_SPIOL | ||||||||
| Accession | Primary (citable) accession number: P52426 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


