ID MDAR3_ARATH Reviewed; 434 AA. AC Q9LFA3; Q8LBV9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-DEC-2008, entry version 48. DE RecName: Full=Probable monodehydroascorbate reductase, cytoplasmic isoform 3; DE Short=MDAR 3; DE EC=1.6.5.4; GN OrderedLocusNames=At3g52880; ORFNames=F8J2_50; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to CC ascorbate, oxidizing NADH in the process (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + 2 monodehydroascorbate = NAD(+) + 2 CC ascorbate. CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). 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; AL132969; CAB86892.1; -; Genomic_DNA. DR EMBL; AF360197; AAK25907.1; -; mRNA. DR EMBL; AY057576; AAL09815.1; -; mRNA. DR EMBL; AY045666; AAK74024.1; -; mRNA. DR EMBL; AY070718; AAL50062.1; -; mRNA. DR EMBL; AY060525; AAL31138.1; -; mRNA. DR EMBL; AY091403; AAM14342.1; -; mRNA. DR EMBL; AY125492; AAM83213.1; -; mRNA. DR EMBL; AY086968; AAM64531.1; -; mRNA. DR PIR; T47545; T47545. DR RefSeq; NP_190856.1; -. DR UniGene; At.24483; -. DR PRIDE; Q9LFA3; -. DR GeneID; 824454; -. DR GenomeReviews; BA000014_GR; AT3G52880. DR KEGG; ath:AT3G52880; -. DR NMPDR; fig|3702.1.peg.16560; -. DR TAIR; At3g52880; -. DR ArrayExpress; Q9LFA3; -. DR GermOnline; AT3G52880; Arabidopsis thaliana. DR GO; GO:0048046; C:apoplast; IDA:TAIR. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0005782; C:peroxisomal matrix; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:EC. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; TAS:TAIR. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009626; P:plant-type hypersensitive response; IDA:TAIR. DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR001100; Pyr_nuc-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 PRINTS; PR00411; PNDRDTASEI. DR ProDom; PD000139; FAD_pyr_redox; 1. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase; KW Redox-active center. FT CHAIN 1 434 Probable monodehydroascorbate reductase, FT cytoplasmic isoform 3. FT /FTId=PRO_0000209138. FT CONFLICT 206 206 D -> N (in Ref. 3; AAM64531). SQ SEQUENCE 434 AA; 46487 MW; DE7FFF0F349784A0 CRC64; MAEKSFKYII LGGGVSAGYA AKEFANQGVQ PGELAVISKE AVAPYERPAL SKGYLFPEGA ARLPGFHCCV GSGGEKLLPE SYKQKGIELI LSTEIVKADL SAKSLVSATG DVFKYQTLII ATGSTVLRLT DFGVKGADSK NILYLREIDD ADKLVEAIKA KKGGKAVVVG GGYIGLELSA VLRINNLDVT MVFPEPWCMP RLFTADIAAF YETYYTNKGV KIIKGTVASG FTAQPNGEVK EVQLKDGRTL EADIVIVGVG AKPLTSLFKG QVEEDKGGIK TDAFFKTSVP DVYAVGDVAT FPLKMYGDVR RVEHVDHSRK SAEQAVKAIK AAEGGAAVEE YDYLPFFYSR SFDLSWQFYG DNVGDSVLFG DSNPSNPKPR FGAYWVQGGK VVGAFMEGGS GDENKALAKV AKARPSAESL DELVKQGISF AAKI //