[1]	PROTEIN SEQUENCE. TISSUE=Fruit; 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).
[2]	CATALYTIC ACTIVITY, AND COFACTOR. TISSUE=Fruit; PubMed=4055727 [NCBI, ExPASy, EBI, Israel, Japan] Hossain M.A., Asada K.; "Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme."; J. Biol. Chem. 260:12920-12926(1985).

Comments

FUNCTION: Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process.
CATALYTIC ACTIVITY: NADH + 2 monodehydroascorbate = NAD⁺ + 2 ascorbate.
COFACTOR: FAD.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=4.6 µM for NADH;
	K_M=23 µM for NADPH;
	K_M=1.4 µM for monodehydroascorbate;
	V_max=256 µmol/min/mg enzyme for NADH oxidation reaction;
	V_max=192 µmol/min/mg enzyme for NADPH oxidation reaction;
pH dependence:	Optimum pH is 7-9;

PTM: The N-terminus is blocked.
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

3D structure databases
ModBase	P83966.
Family and domain databases
InterPro	IPR013027; FAD_pyr_nucl-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.
ProDom	PD000139; FAD_pyr_redox; 1. [Domain structure / List of seq. sharing at least 1 domain]
BLOCKS	P83966.
Other
ProtoNet	P83966.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >166`	`>166`	`Monodehydroascorbate reductase, fruit isozyme.`	`PRO_0000209141`
`UNSURE`	`92 92`		`L or K.`
`NON_CONS`	`13 14`
`NON_CONS`	`32 33`
`NON_CONS`	`58 59`
`NON_CONS`	`92 93`
`NON_CONS`	`128 129`
`NON_CONS`	`135 136`
`NON_CONS`	`150 151`
`NON_TER`	`1 1`
`NON_TER`	`166 166`

Sequence information

Length: 166 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 18811 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 0816E13BF68A6260 [This is a checksum on the sequence]

        10         20         30         40         50         60 
EAVAPYERPA LSKNIFYLRE IADADQLVEA IKLKDGRTLD ADIVVVGVGG RPLVSLFKTS 

        70         80         90        100        110        120 
IPDVYAVGDV ATYPLKLYNE LRRVEHVDHA RLSIEEYDYL PYFYSRTFNL AWQFYGDNVG 

       130        140        150        160 
ETVLFPDNFG TYWIKVVGVF LEGGTPDEYK VARVQPPVES LDQLAK

P83966 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