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Reviewed, UniProtKB/Swiss-Prot Q40977 (MDAR_PEA)

Last modified November 25, 2008. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Monodehydroascorbate reductase
      Short name=MDAR
    EC=1.6.5.4
Alternative name(s):
    Ascorbate free radical reductase
      Short name=AFR reductase
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

monodehydroascorbate reductase (NADH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433Monodehydroascorbate reductase
PRO_0000209143

Regions

Nucleotide binding6 – 2318FAD By similarity
Nucleotide binding164 – 18118NAD By similarity
Nucleotide binding190 – 1945FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q40977-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5435C1F9E2BFCC97

FASTA43347,309
        10         20         30         40         50         60 
MVHSFKYIII GGGVSAGYAA REFVKQGVHP GELAIISKEA VAPYERPALS KAYLFPESPA 

        70         80         90        100        110        120 
RLPGFHTCVG SGGERLLPEW YSEKGIQLYL STEIVSADLA AKFLKSANGE HFDYQTLVIA 

       130        140        150        160        170        180 
TGSAVIRLTD FGVIGANAKN IFYLREVDDA DKLYEAIKRK KNAKRVVVGG GYIGLELSAV 

       190        200        210        220        230        240 
LKLNDLDVTM VYPEPWCMPR LFTSEIAAFY EGYYANKGIN IIKGTVAVGF TANSDGEVKE 

       250        260        270        280        290        300 
VKLKDGRVLE ADIVIVGVGG RPQISLFKGQ VEEQHGGIKT DSFFKTSVPD VYAVGDVATF 

       310        320        330        340        350        360 
PLKLYNDVRR VEHVDHARKS AEQAAKAIFA ADVGKSVEEY DYLPYFYSRS FDLSWQFYGD 

       370        380        390        400        410        420 
NVGETVLFGD NDPASSKPKF GTYWIKEGKV VGAFLEGGTP DENKAIAKVA RAKPAVEDVN 

       430 
QLAEEGLSFA SKI 

« Hide

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.
PIRA55333.

3D structure databases

HSSPHSSP built from PDB template 1ONF based on UniProtKB Q94655.
ModBaseSearch...

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001100. Pyr_nuc-diS_OxRdtase.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00411. PNDRDTASEI.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameMDAR_PEA
AccessionPrimary (citable) accession number: Q40977
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents