Reviewed, UniProtKB/Swiss-Prot Q42711 (MDARS_CUCSA)

Names and origin

Protein names	Recommended name:     Monodehydroascorbate reductase, seedling isozyme       Short name=MDAR seedling     EC=1.6.5.4 Alternative name(s):     Ascorbate free radical reductase seedling       Short name=AFR reductase seedling
Organism	Cucumis sativus (Cucumber)
Taxonomic identifier	3659 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Cucurbitales › Cucurbitaceae › Cucumis

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Monodehydroascorbate reductase, seedling isozyme		PRO_0000209140
Regions
	Nucleotide binding	7 – 24	18	FAD By similarity
	Nucleotide binding	165 – 182	18	NAD By similarity
	Nucleotide binding	191 – 195	5	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q42711-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 302DA61F8C3E4E23	FASTA	434	47,416
	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

References

[1]

"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." Sano S., Asada K. Plant Cell Physiol. 35:425-437(1994) [PubMed: 8055175] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Seedling cotyledon.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D26392 mRNA. Translation: BAA05408.1.
PIR	JU0182.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00411. PNDRDTASEI.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

MDARS_CUCSA

Accession

Primary (citable) accession number: Q42711

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)