ID   MDAR_SOLLC              Reviewed;         433 AA.
AC   Q43497;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 53.
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;
GN   Name=AFRR;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Castlemart; TISSUE=Fruit;
RX   MEDLINE=95303967; PubMed=7784511; DOI=10.1104/pp.108.1.411;
RA   Grantz A.A., Brummell D.A., Bennett A.B.;
RT   "Ascorbate free radical reductase mRNA levels are induced by
RT   wounding.";
RL   Plant Physiol. 108:411-418(1995).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, and to a lesser degree in
CC       stems, roots and all stages of fruit.
CC   -!- INDUCTION: By wounding.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
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DR   EMBL; L41345; AAC41654.1; -; Genomic_DNA.
DR   PIR; T06407; T06407.
DR   HSSP; Q94655; 1ONF.
DR   BRENDA; 1.6.5.4; 281054.
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_0000209142.
FT   NP_BIND       7     24       FAD (By similarity).
FT   NP_BIND     165    182       NAD (By similarity).
FT   NP_BIND     191    195       FAD (By similarity).
SQ   SEQUENCE   433 AA;  47036 MW;  6E3375DB73A1391A CRC64;
     MAEKSFKYVI VGGGVSAGYA AREFAKQGVK PGELAIISKE AVAPYERPAL SKAYLFPEGA
     ARLPGFHVCV GSGGERQLPE WYAEKGISLI LSTEIVKADL ASKTLVSAAG ESFKYQTLVI
     ATGTTVLKLS DFGVQGADSK NIFYLREIDD ADQLVEALKA KKNGKAVVVG GGYIGLELSA
     VLRLNNIEVN MVYPEPWCMP RLFTEGIAAF YEGYYKNKGV NIIKGTVAVG FDTHPNGEVK
     EVKLKDGRVL EADIVVVGVG ARPLTTLFKG QVEEEKGGIK TDAFFKTSVP DVYAVGDVAT
     FPLKMYNEIR RVEHVDHSRK SAEQAVKAIF ASEQGKSVDE YDYLPYFYSR AFDLSWQFYG
     DNVGETVLFG DADPNSATHK FGQYWIKDGK IVGAFLESGS PEENKAIAKV AKVQPPATLD
     QLAQEGISFA SKI
//