Reviewed,
UniProtKB/Swiss-Prot P15719 (MDHP_MAIZE)
Last modified
June 16, 2009.
Version 83.
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 |
| Organism | Zea mays (Maize) |
| Taxonomic identifier | 4577 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea |
Protein attributes
| Sequence length | 432 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. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| 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 |
| PTM | Disulfide bond |
| 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-SubCell |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 40 | 40 | Chloroplast Ref.3 | ||||||||
| Chain | 41 – 432 | 392 | Malate dehydrogenase [NADP], chloroplastic | PRO_0000018643 | |||||||
Regions | |||||||||||
| Nucleotide binding | 96 – 102 | 7 | NADP By similarity | ||||||||
| Nucleotide binding | 214 – 216 | 3 | NADP By similarity | ||||||||
Sites | |||||||||||
| Active site | 272 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 177 | 1 | Substrate By similarity | ||||||||
| Binding site | 183 | 1 | Substrate By similarity | ||||||||
| Binding site | 190 | 1 | NADP By similarity | ||||||||
| Binding site | 197 | 1 | NAD By similarity | ||||||||
| Binding site | 216 | 1 | Substrate By similarity | ||||||||
| Binding site | 247 | 1 | Substrate By similarity | ||||||||
| Site | 67 | 1 | Activation of NADP-MDH | ||||||||
| Site | 72 | 1 | Activation of NADP-MDH | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 67 ↔ 72 | In oxidized inactive NAD-MDH Ref.2 | |||||||||
| Disulfide bond | 408 ↔ 420 | In oxidized inactive NAD-MDH By similarity | |||||||||
Sequences
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References
| [1] | "Maize NADP-malate dehydrogenase: cDNA cloning, sequence, and mRNA characterization." Metzler M., Rothermel B.A., Nelson T. Plant Mol. Biol. 12:713-722(1989) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf. |
| [2] | "Primary structure of the light-dependent regulatory site of corn NADP-malate dehydrogenase." Decottignies P., Schmitter J.-M., Miginiac-Maslow M., le Marechal P., Jacquot J.-P., Gadal P. J. Biol. Chem. 263:11780-11785(1988) [PubMed: 3403553] [Abstract] Cited for: PROTEIN SEQUENCE OF 58-84. |
| [3] | "Amino acid sequence and molecular weight of native NADP malate dehydrogenase from the C4 plant Zea mays." Agostino A., Jeffrey P., Hatch M.D. Plant Physiol. 98:1506-1510(1992) [PubMed: 16668822] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-62. |
Cross-references
Sequence databases | |
|---|---|
| X16084 mRNA. Translation: CAA34213.1. | |
| PIR | DEMZMC. S04859. |
| RefSeq | NP_001105420.1. |
| UniGene | Zm.122 |
3D structure databases | |
| HSSP | HSSP built from PDB template 7MDH based on UniProtKB P17606. |
| SMR | P15719. Positions 64-429. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 542374. |
Organism-specific databases | |
| Gramene | P15719. |
| MaizeGDB | 40092. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.82. 289. |
Family and domain databases | |
| InterPro | IPR001236. Lactate/malate_DH. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR011273. Malate_DH_NADP-dep_pln. IPR010945. Malate_DH_SF1. IPR016040. NAD(P)-bd_dom. [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_MAIZE | ||||||||
| Accession | Primary (citable) accession number: P15719 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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