NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Seedling cotyledon;
PubMed=8055175 [NCBI, ExPASy, EBI, Israel, Japan]
Sano S., Asada K.;
"cDNA cloning of monodehydroascorbate radical reductase from Cucumber: a high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes.";
Plant Cell Physiol. 35:425-437(1994).

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).
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

D26392; BAA05408.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JU0182; JU0182.

3D structure databases

ModBase

Q42711.

Ontologies

GO:0016656;	Molecular function: monodehydroascorbate reductase (NADH) activity (inferred from electronic annotation from EC).
QuickGo view.

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`	`1 434`	`434`	`Monodehydroascorbate reductase, seedling isozyme.`	`PRO_0000209140`
`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: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 47416 Da [This is the MW of the unprocessed precursor]

CRC64: 302DA61F8C3E4E23 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADETFKYVI LGGGVAAGYA AREFVKQGLN PGELAIISKE AVAPYERPAL SKAYLFPESP 

        70         80         90        100        110        120 
ARLPGFHVCV GSGGERLLPD WYKEKGIELI LSTEIVEADL PAKRLRSAHG KIYNYQTLII 

       130        140        150        160        170        180 
ATGSTVIKLS DFGVQGADAK NIFYLREIDD ADQLVEAIKA KENGKVVVVG GGYIGLELGA 

       190        200        210        220        230        240 
ALRINNFDVS MVYPEPWCMP RLFTPEIAAF YEGYYAQKGI TIIKGTVAVG FTVDTNGEVK 

       250        260        270        280        290        300 
EVKLKDGRVL EADIVVVGVG ARPLTSLFKG QIVEEKGGIK TDEFFKTSVP DVYAVGDVAT 

       310        320        330        340        350        360 
FPLKLYNELR RVEHVDHSRK SAEQAVKAIK ASEEGKAIEE YDYLPYFYSR SFDLSWQFYG 

       370        380        390        400        410        420 
DNVGDAVLFG DNSPDSATHK FGSYWIKDGK VVGAFLESGS PEENKAIAKV ARIQPSVESS 

       430 
DLLLKEGISF ASKV

Q42711 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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