ID MDARS_CUCSA Reviewed; 434 AA. AC Q42711; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 48. DE RecName: Full=Monodehydroascorbate reductase, seedling isozyme; DE Short=MDAR seedling; DE EC=1.6.5.4; DE AltName: Full=Ascorbate free radical reductase seedling; DE Short=AFR reductase seedling; OS Cucumis sativus (Cucumber). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucumis. OX NCBI_TaxID=3659; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Seedling cotyledon; RX MEDLINE=94332398; PubMed=8055175; RA Sano S., Asada K.; RT "cDNA cloning of monodehydroascorbate radical reductase from Cucumber: RT a high degree of homology in terms of amino acid sequence between this RT enzyme and bacterial flavoenzymes."; RL Plant Cell Physiol. 35:425-437(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 -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D26392; BAA05408.1; -; mRNA. DR PIR; JU0182; JU0182. DR BRENDA; 1.6.5.4; 1241. 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 2: Evidence at transcript level; KW Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; KW Redox-active center. FT CHAIN 1 434 Monodehydroascorbate reductase, seedling FT isozyme. FT /FTId=PRO_0000209140. 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 434 AA; 47416 MW; 302DA61F8C3E4E23 CRC64; MADETFKYVI LGGGVAAGYA AREFVKQGLN PGELAIISKE AVAPYERPAL SKAYLFPESP ARLPGFHVCV GSGGERLLPD WYKEKGIELI LSTEIVEADL PAKRLRSAHG KIYNYQTLII ATGSTVIKLS DFGVQGADAK NIFYLREIDD ADQLVEAIKA KENGKVVVVG GGYIGLELGA ALRINNFDVS MVYPEPWCMP RLFTPEIAAF YEGYYAQKGI TIIKGTVAVG FTVDTNGEVK EVKLKDGRVL EADIVVVGVG ARPLTSLFKG QIVEEKGGIK TDEFFKTSVP DVYAVGDVAT FPLKLYNELR RVEHVDHSRK SAEQAVKAIK ASEEGKAIEE YDYLPYFYSR SFDLSWQFYG DNVGDAVLFG DNSPDSATHK FGSYWIKDGK VVGAFLESGS PEENKAIAKV ARIQPSVESS DLLLKEGISF ASKV //