MDAR3_ORYSJ
ID MDAR3_ORYSJ Reviewed; 435 AA.
AC Q652L6; Q9XFZ3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Monodehydroascorbate reductase 3, cytosolic {ECO:0000305};
DE Short=OsMDAR3 {ECO:0000303|PubMed:25546583};
DE Short=OsMDHAR3 {ECO:0000303|PubMed:25546583};
DE EC=1.6.5.4 {ECO:0000269|PubMed:24376554, ECO:0000269|PubMed:27652777};
GN Name=MDAR3 {ECO:0000303|PubMed:25546583};
GN Synonyms=MDHAR3 {ECO:0000303|PubMed:25546583};
GN OrderedLocusNames=Os09g0567300 {ECO:0000312|EMBL:BAF25874.1},
GN LOC_Os09g39380 {ECO:0000305};
GN ORFNames=OJ1155_H10.27 {ECO:0000312|EMBL:BAD46251.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RA Kaminaka H., Morita S., Tokumoto M., Masumura T., Tanaka K.;
RT "Molecular cloning and characterization of a cDNA encoding
RT monodehydroascorbate reductase from rice.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24376554; DOI=10.1371/journal.pone.0082611;
RA Wang X., Hargrove M.S.;
RT "Nitric oxide in plants: the roles of ascorbate and hemoglobin.";
RL PLoS ONE 8:E82611-E82611(2013).
RN [6]
RP INDUCTION.
RX PubMed=25546583; DOI=10.1016/j.jplph.2014.09.020;
RA Li Z., Su D., Lei B., Wang F., Geng W., Pan G., Cheng F.;
RT "Transcriptional profile of genes involved in ascorbate glutathione cycle
RT in senescing leaves for an early senescence leaf (esl) rice mutant.";
RL J. Plant Physiol. 176:1-15(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 4-435 IN COMPLEX WITH ASCORBATE;
RP FAD; NAD AND NADP, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF CYS-70;
RP GLY-72; GLU-196; ARG-320; TYR-349 AND ARG-351.
RX PubMed=27652777; DOI=10.1038/srep33903;
RA Park A.K., Kim I.S., Do H., Jeon B.W., Lee C.W., Roh S.J., Shin S.C.,
RA Park H., Kim Y.S., Kim Y.H., Yoon H.S., Lee J.H., Kim H.W.;
RT "Structure and catalytic mechanism of monodehydroascorbate reductase,
RT MDHAR, from Oryza sativa L. japonica.";
RL Sci. Rep. 6:33903-33903(2016).
CC -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to
CC ascorbate, oxidizing NADH in the process. Ascorbate is a major
CC antioxidant against reactive oxygen species (ROS) and nitric oxide (NO)
CC (PubMed:24376554, PubMed:27652777). Can use NADPH as electron donor,
CC but possesses lower activity compared to NADH as electron donor
CC (PubMed:27652777). {ECO:0000269|PubMed:24376554,
CC ECO:0000269|PubMed:27652777}.
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; Evidence={ECO:0000269|PubMed:24376554,
CC ECO:0000269|PubMed:27652777};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:27652777};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Down-regulated during senescence.
CC {ECO:0000269|PubMed:25546583}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; D85764; BAA77214.1; -; mRNA.
DR EMBL; AP005558; BAD46251.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25874.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT09471.1; -; Genomic_DNA.
DR RefSeq; XP_015611766.1; XM_015756280.1.
DR PDB; 5JCI; X-ray; 1.70 A; A=4-435.
DR PDB; 5JCK; X-ray; 2.00 A; A=1-435.
DR PDB; 5JCL; X-ray; 1.80 A; A/B=4-435.
DR PDB; 5JCM; X-ray; 1.90 A; A/B=4-435.
DR PDB; 5JCN; X-ray; 2.29 A; A/B=1-435.
DR PDBsum; 5JCI; -.
DR PDBsum; 5JCK; -.
DR PDBsum; 5JCL; -.
DR PDBsum; 5JCM; -.
DR PDBsum; 5JCN; -.
DR AlphaFoldDB; Q652L6; -.
DR SMR; Q652L6; -.
DR STRING; 4530.OS09T0567300-01; -.
DR PaxDb; Q652L6; -.
DR PRIDE; Q652L6; -.
DR EnsemblPlants; Os09t0567300-01; Os09t0567300-01; Os09g0567300.
DR GeneID; 4347885; -.
DR Gramene; Os09t0567300-01; Os09t0567300-01; Os09g0567300.
DR KEGG; osa:4347885; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_1_1; -.
DR InParanoid; Q652L6; -.
DR OMA; IATYPYH; -.
DR OrthoDB; 405030at2759; -.
DR BRENDA; 1.6.5.4; 8948.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblPlants.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IDA:UniProtKB.
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; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..435
FT /note="Monodehydroascorbate reductase 3, cytosolic"
FT /id="PRO_0000442021"
FT BINDING 14..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 147..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 172..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCK"
FT BINDING 174..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCL"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCK"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCK"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCL"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCK"
FT BINDING 261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCL"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 314..315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCK"
FT BINDING 314..315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCL"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 320
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCN"
FT BINDING 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCI"
FT BINDING 349
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCK"
FT BINDING 349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCL"
FT BINDING 351
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:27652777,
FT ECO:0007744|PDB:5JCN"
FT MUTAGEN 70
FT /note="C->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:27652777"
FT MUTAGEN 70
FT /note="C->S: Slight reduction of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27652777"
FT MUTAGEN 72
FT /note="G->N: Slight reduction of catalytic activity."
FT /evidence="ECO:0000269|PubMed:27652777"
FT MUTAGEN 196
FT /note="E->A: Reduces catalytic activity 2-fold."
FT /evidence="ECO:0000269|PubMed:27652777"
FT MUTAGEN 320
FT /note="R->A: Reduces catalytic activity 5-fold."
FT /evidence="ECO:0000269|PubMed:27652777"
FT MUTAGEN 349
FT /note="Y->A,F,W: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:27652777"
FT MUTAGEN 351
FT /note="R->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:27652777"
FT CONFLICT 257
FT /note="V -> G (in Ref. 1; BAA77214)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5JCI"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5JCI"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5JCN"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5JCI"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:5JCI"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:5JCI"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5JCI"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 316..335
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:5JCL"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:5JCI"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 421..426
FT /evidence="ECO:0007829|PDB:5JCI"
FT HELIX 428..434
FT /evidence="ECO:0007829|PDB:5JCI"
SQ SEQUENCE 435 AA; 46673 MW; E0771D77F9A2D36E CRC64;
MASEKHFKYV ILGGGVAAGY AAREFAKQGV KPGELAIISK EAVAPYERPA LSKGYLFPQN
AARLPGFHVC VGSGGERLLP EWYSEKGIEL ILSTEIVKAD LASKTLTSAV GATFTYEILI
IATGSSVIKL SDFGTQGADS NNILYLREVD DADKLVAAIQ AKKGGKAVIV GGGYIGLELS
AALKINDFDV TMVFPEPWCM PRLFTADIAA FYESYYTNKG VKIVKGTVAV GFDADANGDV
TAVNLKNGSV LEADIVVVGV GGRPLTTLFK GQVAEEKGGI KTDAFFETSV PGVYAVGDVA
TFPMKMYNEL RRVEHVDHAR KSAEQAVKAI KGKESGESVV EYDYLPYFYS RSFDLGWQFY
GDNVGDTILF GDSDPTSAKP KFGSYWIKDG KVLGAFLEGG SPDENKAIAK VAKTQPPVAN
IEELKKEGLQ FASKI
