Reviewed, UniProtKB/Swiss-Prot Q40977 (MDAR_PEA)

Names and origin

Protein names	Recommended name:     Monodehydroascorbate reductase       Short name=MDAR     EC=1.6.5.4 Alternative name(s):     Ascorbate free radical reductase       Short name=AFR reductase
Organism	Pisum sativum (Garden pea)
Taxonomic identifier	3888 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 at relatively low levels in all tissues examined. Ref.1
Sequence similarities	Belongs to the FAD-dependent oxidoreductase family.
biophysicochemical properties	Kinetic parameters: KM=5.3 µM for NADH KM=21.5 µM for NADPH KM=5.7 µM for monodehydroascorbate Vmax=312 µmol/min/mg enzyme for NADH oxidation reaction Vmax=40.9 µmol/min/mg enzyme for NADPH oxidation reaction pH dependence: Optimum pH is 7.5-9.5.

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-SubCell
Molecular function	FAD binding 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 – 433	433	Monodehydroascorbate reductase		PRO_0000209143
Regions
	Nucleotide binding	6 – 23	18	FAD By similarity UniProtKB P42454
	Nucleotide binding	164 – 181	18	NAD By similarity UniProtKB P42454
	Nucleotide binding	190 – 194	5	FAD By similarity UniProtKB P42454

Sequences

	Sequence		Length	Mass (Da)
	Q40977-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5435C1F9E2BFCC97	FASTA	433	47,309
	10 20 30 40 50 60 MVHSFKYIII GGGVSAGYAA REFVKQGVHP GELAIISKEA VAPYERPALS KAYLFPESPA 70 80 90 100 110 120 RLPGFHTCVG SGGERLLPEW YSEKGIQLYL STEIVSADLA AKFLKSANGE HFDYQTLVIA 130 140 150 160 170 180 TGSAVIRLTD FGVIGANAKN IFYLREVDDA DKLYEAIKRK KNAKRVVVGG GYIGLELSAV 190 200 210 220 230 240 LKLNDLDVTM VYPEPWCMPR LFTSEIAAFY EGYYANKGIN IIKGTVAVGF TANSDGEVKE 250 260 270 280 290 300 VKLKDGRVLE ADIVIVGVGG RPQISLFKGQ VEEQHGGIKT DSFFKTSVPD VYAVGDVATF 310 320 330 340 350 360 PLKLYNDVRR VEHVDHARKS AEQAAKAIFA ADVGKSVEEY DYLPYFYSRS FDLSWQFYGD 370 380 390 400 410 420 NVGETVLFGD NDPASSKPKF GTYWIKEGKV VGAFLEGGTP DENKAIAKVA RAKPAVEDVN 430 QLAEEGLSFA SKI

References

[1]	"Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase." Murthy S.S., Zilinskas B.A. J. Biol. Chem. 269:31129-31133(1994) [PubMed: 7983054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U06461 mRNA. Translation: AAA60979.1.
PIR	A55333.
3D structure databases
HSSP	HSSP built from PDB template 1ONF based on UniProtKB Q94655.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.5.4. 287.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-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.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

MDAR_PEA

Accession

Primary (citable) accession number: Q40977

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)