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Q43497 (MDAR_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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) [Reference proteome]
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
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. Ref.1

Cofactor

FAD By similarity.

Subcellular location

Cytoplasm Probable Ref.1.

Tissue specificity

Expressed in leaves, and to a lesser degree in stems, roots and all stages of fruit. Ref.1

Induction

By wounding. Ref.1

Sequence similarities

Belongs to the FAD-dependent oxidoreductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionflavin adenine dinucleotide binding

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 UniProtKB P42454
Nucleotide binding165 – 18218NAD By similarity UniProtKB P42454
Nucleotide binding191 – 1955FAD By similarity UniProtKB P42454

Sequences

Sequence LengthMass (Da)Tools
Q43497 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Castlemart.
Tissue: Fruit.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L41345 Genomic DNA. Translation: AAC41654.1.
PIRT06407.

3D structure databases

ProteinModelPortalQ43497.
ModBaseSearch...

Proteomic databases

PRIDEQ43497.
ProMEXQ43497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
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: April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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