MDAR_ARATH
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 03-AUG-2022, entry version 149.
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},
GN MDHAR6 {ECO:0000303|PubMed:26339024},
GN 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 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 [5]
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 [6]
RP FUNCTION, 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 [7]
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, BIOTECHNOLOGY, DISRUPTION PHENOTYPE, AND
RP 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. Can also use 2,4,6-
CC trinitrotoluene (TNT) and 1-chloro-2,4-dinitrobenzene (CDNB) as
CC substrates, but not 1-chloro-4-nitrobenzene (CNB).
CC {ECO:0000269|PubMed:16146528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 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 -!- 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=190 mmol/min/mg enzyme with monodehydroascorbate as substrate
CC {ECO:0000269|PubMed:26339024};
CC Vmax=0.960 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, but enhanced 2,4,6-
CC trinitrotoluene (TNT) tolerance. {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; 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 IntAct; P92947; 2.
DR STRING; 3702.AT1G63940.2; -.
DR iPTMnet; P92947; -.
DR PaxDb; P92947; -.
DR PRIDE; P92947; -.
DR ProteomicsDB; 238765; -. [P92947-1]
DR EnsemblPlants; AT1G63940.1; AT1G63940.1; AT1G63940. [P92947-2]
DR EnsemblPlants; AT1G63940.2; AT1G63940.2; AT1G63940. [P92947-1]
DR GeneID; 842697; -.
DR Gramene; AT1G63940.1; AT1G63940.1; AT1G63940. [P92947-2]
DR Gramene; AT1G63940.2; AT1G63940.2; AT1G63940. [P92947-1]
DR KEGG; ath:AT1G63940; -.
DR Araport; AT1G63940; -.
DR TAIR; locus:2195503; AT1G63940.
DR eggNOG; KOG1336; Eukaryota.
DR InParanoid; P92947; -.
DR PhylomeDB; P92947; -.
DR BioCyc; ARA:AT1G63940-MON; -.
DR BRENDA; 1.6.5.4; 399.
DR SABIO-RK; P92947; -.
DR PRO; PR:P92947; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92947; baseline and differential.
DR Genevisible; P92947; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 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
