Reviewed,
UniProtKB/Swiss-Prot Q40977 (MDAR_PEA)
Last modified
November 25, 2008.
Version 46.
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 Short name=MDAR EC=1.6.5.4 Alternative name(s): Ascorbate free radical reductase Short name=AFR reductase |
| Organism | Pisum sativum (Garden pea) |
| Taxonomic identifier | 3888 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum |
Protein attributes
| Sequence length | 433 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Cofactor | FAD By similarity. |
| Subcellular location | CytoplasmProbable. |
| Tissue specificity | Expressed at relatively low levels in all tissues examined. |
| Sequence similarities | Belongs to the FAD-dependent oxidoreductase family. |
| Biophysicochemical properties | Kinetic parameters: KM=5.3 µM for NADH KM=21.5 µM for NADPH KM=5.7 µM for monodehydroascorbate Vmax=312 µmol/min/mg enzyme for NADH oxidation reaction Vmax=40.9 µmol/min/mg enzyme for NADPH oxidation reaction pH dependence: Optimum pH is 7.5-9.5. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro monodehydroascorbate reductase (NADH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase." Murthy S.S., Zilinskas B.A. J. Biol. Chem. 269:31129-31133(1994) [PubMed: 7983054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Leaf. |
Cross-references
Sequence databases | |
|---|---|
| U06461 mRNA. Translation: AAA60979.1. | |
| PIR | A55333. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ONF based on UniProtKB Q94655. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00411. PNDRDTASEI. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | MDAR_PEA | ||||||||
| Accession | Primary (citable) accession number: Q40977 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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