Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Monodehydroascorbate reductase

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process.

Catalytic activityi

NADH + 2 monodehydroascorbate = NAD+ + 2 ascorbate.1 Publication

Cofactori

FADUniRule annotationBy similarity

Kineticsi

  1. KM=5.3 µM for NADH
  2. KM=21.5 µM for NADPH
  3. KM=5.7 µM for monodehydroascorbate
  1. Vmax=312 µmol/min/mg enzyme for NADH oxidation reaction
  2. Vmax=40.9 µmol/min/mg enzyme for NADPH oxidation reaction

pH dependencei

Optimum pH is 7.5-9.5.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 2318FADBy similarityAdd
BLAST
Nucleotide bindingi164 – 18118NADBy similarityAdd
BLAST
Nucleotide bindingi190 – 1945FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Monodehydroascorbate reductase (EC:1.6.5.4)
Short name:
MDAR
Alternative name(s):
Ascorbate free radical reductase
Short name:
AFR reductase
OrganismiPisum sativum (Garden pea)Imported
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Monodehydroascorbate reductasePRO_0000209143Add
BLAST

Proteomic databases

PRIDEiQ40977.

Expressioni

Tissue specificityi

Expressed at relatively low levels in all tissues examined.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ40977.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.

Sequencei

Sequence statusi: Complete.

Q40977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHSFKYIII GGGVSAGYAA REFVKQGVHP GELAIISKEA VAPYERPALS
60 70 80 90 100
KAYLFPESPA RLPGFHTCVG SGGERLLPEW YSEKGIQLYL STEIVSADLA
110 120 130 140 150
AKFLKSANGE HFDYQTLVIA TGSAVIRLTD FGVIGANAKN IFYLREVDDA
160 170 180 190 200
DKLYEAIKRK KNAKRVVVGG GYIGLELSAV LKLNDLDVTM VYPEPWCMPR
210 220 230 240 250
LFTSEIAAFY EGYYANKGIN IIKGTVAVGF TANSDGEVKE VKLKDGRVLE
260 270 280 290 300
ADIVIVGVGG RPQISLFKGQ VEEQHGGIKT DSFFKTSVPD VYAVGDVATF
310 320 330 340 350
PLKLYNDVRR VEHVDHARKS AEQAAKAIFA ADVGKSVEEY DYLPYFYSRS
360 370 380 390 400
FDLSWQFYGD NVGETVLFGD NDPASSKPKF GTYWIKEGKV VGAFLEGGTP
410 420 430
DENKAIAKVA RAKPAVEDVN QLAEEGLSFA SKI
Length:433
Mass (Da):47,309
Last modified:November 1, 1996 - v1
Checksum:i5435C1F9E2BFCC97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06461 mRNA. Translation: AAA60979.1.
PIRiA55333.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06461 mRNA. Translation: AAA60979.1.
PIRiA55333.

3D structure databases

ProteinModelPortaliQ40977.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ40977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Leaf1 Publication.

Entry informationi

Entry nameiMDAR_PEA
AccessioniPrimary (citable) accession number: Q40977
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.