ID   MDAR_ARATH              Reviewed;         493 AA.
AC   P92947; Q94CE2; Q9CAK5;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Monodehydroascorbate reductase, chloroplastic/mitochondrial {ECO:0000303|PubMed:16146528};
DE            EC=1.6.5.4 {ECO:0000269|PubMed:26339024};
DE   AltName: Full=Monodehydroascorbate reductase 5, mitochondrial {ECO:0000303|PubMed:16146528};
DE            Short=AtMDAR5 {ECO:0000303|PubMed:16146528};
DE   AltName: Full=Monodehydroascorbate reductase 6, chloroplastic {ECO:0000303|PubMed:16146528};
DE            Short=AtMDAR6 {ECO:0000303|PubMed:16146528};
DE   Flags: Precursor;
GN   Name=MDAR5 {ECO:0000303|PubMed:16146528};
GN   Synonyms=MDAR6 {ECO:0000303|PubMed:16146528}, MDHAR6
GN   {ECO:0000303|PubMed:26339024}, PMDAR-L {ECO:0000303|PubMed:12154132},
GN   PMDAR-S {ECO:0000303|PubMed:12154132};
GN   OrderedLocusNames=At1g63940 {ECO:0000312|Araport:AT1G63940};
GN   ORFNames=T12P18.4 {ECO:0000312|EMBL:AAG52455.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MDAR5).
RA   Hossain A., Miyake C., Aoki H., Matsuo M., Yamaguchi T., Nishimura M.,
RA   Ida S., Asada K.;
RT   "cDNA of chloroplastic monodehydroascorbate radical reductase from
RT   Arabidopsis thaliana.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MDAR5 AND MDAR6).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   ALTERNATIVE SPLICING (ISOFORMS MDAR5 AND MDAR6), AND SUBCELLULAR
RP   LOCATION(ISOFORMS MDAR5 AND MDAR6).
RX   PubMed=12154132; DOI=10.1093/pcp/pcf103;
RA   Obara K., Sumi K., Fukuda H.;
RT   "The use of multiple transcription starts causes the dual targeting of
RT   Arabidopsis putative monodehydroascorbate reductase to both mitochondria
RT   and chloroplasts.";
RL   Plant Cell Physiol. 43:697-705(2002).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16146528; DOI=10.1111/j.1365-313x.2005.02503.x;
RA   Lisenbee C.S., Lingard M.J., Trelease R.N.;
RT   "Arabidopsis peroxisomes possess functionally redundant membrane and matrix
RT   isoforms of monodehydroascorbate reductase.";
RL   Plant J. 43:900-914(2005).
RN   [8]
RP   INTERACTION WITH TRXY, AND ACTIVITY REGULATION.
RX   PubMed=20405473; DOI=10.1002/pmic.200900835;
RA   Marchand C.H., Vanacker H., Collin V., Issakidis-Bourguet E.,
RA   Marechal P.L., Decottignies P.;
RT   "Thioredoxin targets in Arabidopsis roots.";
RL   Proteomics 10:2418-2428(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   LEU-51.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOTECHNOLOGY,
RP   DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=26339024; DOI=10.1126/science.aab3472;
RA   Johnston E.J., Rylott E.L., Beynon E., Lorenz A., Chechik V., Bruce N.C.;
RT   "Monodehydroascorbate reductase mediates TNT toxicity in plants.";
RL   Science 349:1072-1075(2015).
CC   -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate (MDA) to
CC       ascorbate, oxidizing NADH in the process (PubMed:26339024). Mediates
CC       phytotoxicity of 2,4,6-trinitrotoluene (TNT), an explosive and
CC       environmental pollutant, by reducing TNT and forming a nitro radical
CC       that spontaneously reacts with atmospheric oxygen, generating reactive
CC       superoxide (PubMed:26339024). Can also use 1-chloro-2,4-dinitrobenzene
CC       (CDNB) as substrate, but not 1-chloro-4-nitrobenzene (CNB)
CC       (PubMed:26339024). {ECO:0000269|PubMed:26339024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 monodehydro-L-ascorbate radical + NADH + H(+) = 2 L-
CC         ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:59513; EC=1.6.5.4;
CC         Evidence={ECO:0000269|PubMed:26339024};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14582;
CC         Evidence={ECO:0000269|PubMed:26339024};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4,6-trinitrotoluene + NADH = 2,4,6-trinitrotoluene radical +
CC         e(-) + NAD(+); Xref=Rhea:RHEA:80511, ChEBI:CHEBI:10545,
CC         ChEBI:CHEBI:46053, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:231530; Evidence={ECO:0000269|PubMed:26339024};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:80512;
CC         Evidence={ECO:0000269|PubMed:26339024};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9S926};
CC   -!- ACTIVITY REGULATION: Redox regulation of the activity by thioredoxin
CC       TRXy1. {ECO:0000269|PubMed:20405473}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=522 uM for 2,4,6-trinitrotoluene {ECO:0000269|PubMed:26339024};
CC         KM=4.1 uM for monodehydroascorbate {ECO:0000269|PubMed:26339024};
CC         KM=1254 uM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:26339024};
CC         Vmax=0.143 mmol/min/mg enzyme with 2,4,6-trinitrotoluene as substrate
CC         {ECO:0000269|PubMed:26339024};
CC         Vmax=109 mmol/min/mg enzyme with monodehydroascorbate as substrate
CC         {ECO:0000269|PubMed:26339024};
CC         Vmax=0.96 mmol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC         substrate {ECO:0000269|PubMed:26339024};
CC   -!- SUBUNIT: Interacts in vitro with TRXy. {ECO:0000269|PubMed:20405473}.
CC   -!- SUBCELLULAR LOCATION: [Isoform MDAR6]: Plastid, chloroplast
CC       {ECO:0000269|PubMed:12154132}.
CC   -!- SUBCELLULAR LOCATION: [Isoform MDAR5]: Mitochondrion
CC       {ECO:0000269|PubMed:12154132, ECO:0000305|PubMed:25732537}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=MDAR5; Synonyms=PMDAR-L;
CC         IsoId=P92947-1; Sequence=Displayed;
CC       Name=MDAR6; Synonyms=PMDAR-S;
CC         IsoId=P92947-2; Sequence=VSP_011360;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal conditions, but
CC       enhanced 2,4,6-trinitrotoluene (TNT) tolerance.
CC       {ECO:0000269|PubMed:26339024}.
CC   -!- BIOTECHNOLOGY: The main mechanism for TNT toxicity in plants is the
CC       production of superoxide in the mitochondria by MDAR5 with TNT as a
CC       substrate. Inactivation of MDAR5 enhance TNT tolerance, thus enabling
CC       revegetation and remediation of explosives-contaminated sites.
CC       {ECO:0000269|PubMed:26339024}.
CC   -!- MISCELLANEOUS: The use of alternative transcription starts causes dual
CC       targeting of the same mature MDAR protein to both mitochondria and
CC       chloroplast. {ECO:0000269|PubMed:12154132}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; D84417; BAA12349.2; -; mRNA.
DR   EMBL; AC010852; AAG52455.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34168.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34171.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7031992.1; -; Genomic_DNA.
DR   EMBL; AY034934; AAK59441.1; -; mRNA.
DR   EMBL; AY142572; AAN13141.1; -; mRNA.
DR   EMBL; BT000667; AAN31814.1; -; mRNA.
DR   PIR; E96664; E96664.
DR   RefSeq; NP_564818.1; NM_105067.4. [P92947-2]
DR   RefSeq; NP_849839.1; NM_179508.3. [P92947-1]
DR   AlphaFoldDB; P92947; -.
DR   SMR; P92947; -.
DR   BioGRID; 27918; 16.
DR   FunCoup; P92947; 1026.
DR   IntAct; P92947; 3.
DR   STRING; 3702.P92947; -.
DR   iPTMnet; P92947; -.
DR   PaxDb; 3702-P92947; -.
DR   ProteomicsDB; 238765; -. [P92947-1]
DR   GeneID; 842697; -.
DR   KEGG; ath:AT1G63940; -.
DR   Araport; AT1G63940; -.
DR   TAIR; AT1G63940; MDAR6.
DR   eggNOG; KOG1336; Eukaryota.
DR   InParanoid; P92947; -.
DR   PhylomeDB; P92947; -.
DR   BioCyc; ARA:AT1G63940-MONOMER; -.
DR   BRENDA; 1.6.5.4; 399.
DR   SABIO-RK; P92947; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   PRO; PR:P92947; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P92947; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0010319; C:stromule; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; EXP:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   FunFam; 3.30.390.30:FF:000018; Monodehydroascorbate reductase; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR050446; FAD-oxidoreductase/Apoptosis.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR048618; MDHAR3-like_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF6; MONODEHYDROASCORBATE REDUCTASE, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   Pfam; PF21791; MDHAR3-like_C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Chloroplast; FAD; Flavoprotein; Mitochondrion;
KW   NAD; NADP; Oxidoreductase; Plastid; Redox-active center;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000305|PubMed:25732537"
FT   CHAIN           52..493
FT                   /note="Monodehydroascorbate reductase,
FT                   chloroplastic/mitochondrial"
FT                   /id="PRO_0000018621"
FT   BINDING         68..71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         95
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         102
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         107
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         201..202
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         224..230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         226..230
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         248
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         254
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         254
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         313
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         313
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         351
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         367..368
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         367..368
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         369
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         373
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         398
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         398
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         398
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   BINDING         400
FT                   /ligand="L-ascorbate"
FT                   /ligand_id="ChEBI:CHEBI:38290"
FT                   /evidence="ECO:0000250|UniProtKB:Q652L6"
FT   VAR_SEQ         1..7
FT                   /note="Missing (in isoform MDAR6)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_011360"
FT   CONFLICT        109
FT                   /note="Y -> H (in Ref. 1; BAA12349)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  53302 MW;  44FBF0DE65DA89D7 CRC64;
     MSAVRRVMAL ASTTLPTKSG LSLWCPSSPS LARRFPARFS PIGSRIASRS LVTASFANEN
     REFVIVGGGN AAGYAARTFV ENGMADGRLC IVTKEAYAPY ERPALTKAYL FPPEKKPARL
     PGFHTCVGGG GERQTPDWYK EKGIEVIYED PVAGADFEKQ TLTTDAGKQL KYGSLIIATG
     CTASRFPDKI GGHLPGVHYI REVADADSLI ASLGKAKKIV IVGGGYIGME VAAAAVAWNL
     DTTIVFPEDQ LLQRLFTPSL AQKYEELYRQ NGVKFVKGAS INNLEAGSDG RVSAVKLADG
     STIEADTVVI GIGAKPAIGP FETLAMNKSI GGIQVDGLFR TSTPGIFAIG DVAAFPLKIY
     DRMTRVEHVD HARRSAQHCV KSLLTAHTDT YDYLPYFYSR VFEYEGSPRK VWWQFFGDNV
     GETVEVGNFD PKIATFWIES GRLKGVLVES GSPEEFQLLP KLARSQPLVD KAKLASASSV
     EEALEIAQAA LQS
//