MDAR5_ORYSJ
ID MDAR5_ORYSJ Reviewed; 491 AA.
AC Q84PW3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Monodehydroascorbate reductase 5, chlorplastic {ECO:0000305};
DE Short=OsMADR5 {ECO:0000303|PubMed:25546583};
DE Short=OsMDHAR5 {ECO:0000303|PubMed:25546583};
DE EC=1.6.5.4 {ECO:0000250|UniProtKB:Q652L6};
DE Flags: Precursor;
GN Name=MDAR5 {ECO:0000303|PubMed:25546583};
GN Synonyms=MDHAR5 {ECO:0000303|PubMed:25546583};
GN OrderedLocusNames=Os08g0151800 {ECO:0000312|EMBL:BAF22916.1},
GN LOC_Os08g05570 {ECO:0000305};
GN ORFNames=OJ1349_D05.106 {ECO:0000312|EMBL:BAC99756.1},
GN P0443G08.138 {ECO:0000312|EMBL:BAC98552.1};
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 [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 [2]
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 [3]
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 [4]
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).
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
CC (NO). {ECO:0000250|UniProtKB:Q652L6}.
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:0000250|UniProtKB:Q652L6};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q652L6};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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; AP004461; BAC98552.1; -; Genomic_DNA.
DR EMBL; AP005467; BAC99756.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF22916.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT03846.1; -; Genomic_DNA.
DR RefSeq; XP_015649952.1; XM_015794466.1.
DR AlphaFoldDB; Q84PW3; -.
DR SMR; Q84PW3; -.
DR STRING; 4530.OS08T0151800-01; -.
DR CarbonylDB; Q84PW3; -.
DR PaxDb; Q84PW3; -.
DR PRIDE; Q84PW3; -.
DR EnsemblPlants; Os08t0151800-01; Os08t0151800-01; Os08g0151800.
DR GeneID; 4344670; -.
DR Gramene; Os08t0151800-01; Os08t0151800-01; Os08g0151800.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_1_1; -.
DR InParanoid; Q84PW3; -.
DR OMA; VMEVASY; -.
DR OrthoDB; 405030at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR GO; GO:0010319; C:stromule; IEA:EnsemblPlants.
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; IEA:EnsemblPlants.
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.
PE 2: Evidence at transcript level;
KW Chloroplast; FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Plastid;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..491
FT /note="Monodehydroascorbate reductase 5, chlorplastic"
FT /id="PRO_0000442023"
FT BINDING 61..64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 88
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 100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 194..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 217..223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 219..223
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 306
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 344
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 360..361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 360..361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 362
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 366
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 391
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 393
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
SQ SEQUENCE 491 AA; 52759 MW; 42EC26DD48670BD1 CRC64;
MASTAAAASS QGCISWALRQ RGLGGGGARA VPVLPRRRFC VSAAAGAGFD NENREYVIVG
GGNAAGYAAR TFVEHGMADG RLCIVSKEAY PPYERPALTK GYLFPPDKKP ARLPGFHTCV
GSGGQRQTAE WYKENGIEVL YEDPVVAFDG KTHTLKTSSG KILKYGSLII STGCEASRLP
AKIGGNLPGV HYIRDVADAD SLVSSLGKAK KIVVIGGGYI GMEVAAAACG WNLDTTIIFP
EDHIMPRLFT PSLAKKYEEL YQQNGVKFIK GALIDKLEAG SDGRVSSAVL EDGSVVEADT
VIVGIGARPV IGPFEAVGVN TKVGGIEVDS LFRTSIPGIF AIGDVAAFPL KMYDRMTRVE
HVDHARKSAH HCVEALLTSH TKPYDYLPYF YSRVFEYEGS SRKIWWQFYG DNVGETIEVG
SFEPKIATFW IDSDSRLKGV FLESGSSEEF SLLPQLAKSQ PVVDKAKLKS ATSVEDALEI
ARSSLHSGSS V
