Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q43497 (MDAR_SOLLC)

Last modified November 25, 2008. Version 48. 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
Gene names
Name: AFRR
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

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 in leaves, and to a lesser degree in stems, roots and all stages of fruit.

Induction

By wounding.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase family.

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_0000209142

Regions

Nucleotide binding7 – 2418FAD By similarity
Nucleotide binding165 – 18218NAD By similarity
Nucleotide binding191 – 1955FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43497-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6E3375DB73A1391A

FASTA43347,036
        10         20         30         40         50         60 
MAEKSFKYVI VGGGVSAGYA AREFAKQGVK PGELAIISKE AVAPYERPAL SKAYLFPEGA 

        70         80         90        100        110        120 
ARLPGFHVCV GSGGERQLPE WYAEKGISLI LSTEIVKADL ASKTLVSAAG ESFKYQTLVI 

       130        140        150        160        170        180 
ATGTTVLKLS DFGVQGADSK NIFYLREIDD ADQLVEALKA KKNGKAVVVG GGYIGLELSA 

       190        200        210        220        230        240 
VLRLNNIEVN MVYPEPWCMP RLFTEGIAAF YEGYYKNKGV NIIKGTVAVG FDTHPNGEVK 

       250        260        270        280        290        300 
EVKLKDGRVL EADIVVVGVG ARPLTTLFKG QVEEEKGGIK TDAFFKTSVP DVYAVGDVAT 

       310        320        330        340        350        360 
FPLKMYNEIR RVEHVDHSRK SAEQAVKAIF ASEQGKSVDE YDYLPYFYSR AFDLSWQFYG 

       370        380        390        400        410        420 
DNVGETVLFG DADPNSATHK FGQYWIKDGK IVGAFLESGS PEENKAIAKV AKVQPPATLD 

       430 
QLAQEGISFA SKI 

« Hide

References

[1]"Ascorbate free radical reductase mRNA levels are induced by wounding."
Grantz A.A., Brummell D.A., Bennett A.B.
Plant Physiol. 108:411-418(1995) [PubMed: 7784511] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Castlemart.
Tissue: Fruit.

Cross-references

Sequence databases

L41345 Genomic DNA. Translation: AAC41654.1.
PIRT06407.

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_SOLLC
AccessionPrimary (citable) accession number: Q43497
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 48 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