NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Castlemart;
TISSUE=Fruit;
DOI=10.1104/pp.108.1.411; PubMed=7784511 [NCBI, ExPASy, EBI, Israel, Japan]
Grantz A.A., Brummell D.A., Bennett A.B.;
"Ascorbate free radical reductase mRNA levels are induced by wounding.";
Plant Physiol. 108:411-418(1995).

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: Cytoplasm (Probable).
TISSUE SPECIFICITY: Expressed in leaves, and to a lesser degree in stems, roots and all stages of fruit.
INDUCTION: By wounding.
SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L41345; AAC41654.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T06407; T06407.

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

ModBase

Q43497.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 433`	`433`	`Monodehydroascorbate reductase.`	`PRO_0000209142`
`NP_BIND`	`7 24`	`18`	`FAD (By similarity).`
`NP_BIND`	`165 182`	`18`	`NAD (By similarity).`
`NP_BIND`	`191 195`	`5`	`FAD (By similarity).`

Sequence information

Length: 433 AA [This is the length of the unprocessed precursor]

Molecular weight: 47036 Da [This is the MW of the unprocessed precursor]

CRC64: 6E3375DB73A1391A [This is a checksum on the sequence]

        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

Q43497 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools