Reviewed,
UniProtKB/Swiss-Prot P83966 (MDARF_CUCSA)
Last modified
February 9, 2010.
Version 28.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Monodehydroascorbate reductase, fruit isozyme Short name=MDAR fruit EC=1.6.5.4 Alternative name(s): Ascorbate free radical reductase fruit Short name=AFR reductase fruit |
| Organism | Cucumis sativus (Cucumber) |
| Taxonomic identifier | 3659 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Cucumis |
Protein attributes
| Sequence length | 166 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process. |
| Catalytic activity | NADH + 2 monodehydroascorbate = NAD+ + 2 ascorbate. Ref.2 |
| Cofactor | FAD. Ref.2 |
| Post-translational modification | The N-terminus is blocked. Ref.1 |
| Sequence similarities | Belongs to the FAD-dependent oxidoreductase family. |
| Biophysicochemical properties | Kinetic parameters: KM=4.6 µM for NADH KM=23 µM for NADPH KM=1.4 µM for monodehydroascorbate Vmax=256 µmol/min/mg enzyme for NADH oxidation reaction Vmax=192 µmol/min/mg enzyme for NADPH oxidation reaction pH dependence: Optimum pH is 7-9. |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro monodehydroascorbate reductase (NADH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›166 | ›166 | Monodehydroascorbate reductase, fruit isozyme | PRO_0000209141 | |||||
Experimental info | |||||||||
| Sequence uncertainty | 92 | 1 | L or K Ref.1 | ||||||
| Non-adjacent residues | 13 – 14 | 2 | |||||||
| Non-adjacent residues | 32 – 33 | 2 | |||||||
| Non-adjacent residues | 58 – 59 | 2 | |||||||
| Non-adjacent residues | 92 – 93 | 2 | |||||||
| Non-adjacent residues | 128 – 129 | 2 | |||||||
| Non-adjacent residues | 135 – 136 | 2 | |||||||
| Non-adjacent residues | 150 – 151 | 2 | |||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 166 | 1 | |||||||
Sequences
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References
| [1] | "cDNA cloning of monodehydroascorbate radical reductase from Cucumber: a high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes." Sano S., Asada K. Plant Cell Physiol. 35:425-437(1994) [PubMed: 8055175] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Fruit. |
| [2] | "Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme." Hossain M.A., Asada K. J. Biol. Chem. 260:12920-12926(1985) [PubMed: 4055727] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR. Tissue: Fruit. |
Cross-references
Entry information
| Entry name | MDARF_CUCSA | ||||||||
| Accession | Primary (citable) accession number: P83966 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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