ID   MDAR_PEA                Reviewed;         433 AA.
AC   Q40977;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Monodehydroascorbate reductase;
DE            Short=MDAR;
DE            EC=1.6.5.4;
DE   AltName: Full=Ascorbate free radical reductase;
DE            Short=AFR reductase;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Leaf;
RX   MEDLINE=95074153; PubMed=7983054;
RA   Murthy S.S., Zilinskas B.A.;
RT   "Molecular cloning and characterization of a cDNA encoding pea
RT   monodehydroascorbate reductase.";
RL   J. Biol. Chem. 269:31129-31133(1994).
CC   -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to
CC       ascorbate, oxidizing NADH in the process.
CC   -!- CATALYTIC ACTIVITY: NADH + 2 monodehydroascorbate = NAD(+) + 2
CC       ascorbate.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.3 uM for NADH;
CC         KM=21.5 uM for NADPH;
CC         KM=5.7 uM for monodehydroascorbate;
CC         Vmax=312 umol/min/mg enzyme for NADH oxidation reaction;
CC         Vmax=40.9 umol/min/mg enzyme for NADPH oxidation reaction;
CC       pH dependence:
CC         Optimum pH is 7.5-9.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed at relatively low levels in all
CC       tissues examined.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
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DR   EMBL; U06461; AAA60979.1; -; mRNA.
DR   PIR; A55333; A55333.
DR   HSSP; Q94655; 1ONF.
DR   BRENDA; 1.6.5.4; 287.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    433       Monodehydroascorbate reductase.
FT                                /FTId=PRO_0000209143.
FT   NP_BIND       6     23       FAD (By similarity).
FT   NP_BIND     164    181       NAD (By similarity).
FT   NP_BIND     190    194       FAD (By similarity).
SQ   SEQUENCE   433 AA;  47309 MW;  5435C1F9E2BFCC97 CRC64;
     MVHSFKYIII GGGVSAGYAA REFVKQGVHP GELAIISKEA VAPYERPALS KAYLFPESPA
     RLPGFHTCVG SGGERLLPEW YSEKGIQLYL STEIVSADLA AKFLKSANGE HFDYQTLVIA
     TGSAVIRLTD FGVIGANAKN IFYLREVDDA DKLYEAIKRK KNAKRVVVGG GYIGLELSAV
     LKLNDLDVTM VYPEPWCMPR LFTSEIAAFY EGYYANKGIN IIKGTVAVGF TANSDGEVKE
     VKLKDGRVLE ADIVIVGVGG RPQISLFKGQ VEEQHGGIKT DSFFKTSVPD VYAVGDVATF
     PLKLYNDVRR VEHVDHARKS AEQAAKAIFA ADVGKSVEEY DYLPYFYSRS FDLSWQFYGD
     NVGETVLFGD NDPASSKPKF GTYWIKEGKV VGAFLEGGTP DENKAIAKVA RAKPAVEDVN
     QLAEEGLSFA SKI
//