MDAR_SOLLC
ID MDAR_SOLLC Reviewed; 433 AA.
AC Q43497;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Monodehydroascorbate reductase;
DE Short=MDAR;
DE EC=1.6.5.4;
DE AltName: Full=Ascorbate free radical reductase;
DE Short=AFR reductase;
GN Name=AFRR {ECO:0000312|EMBL:AAC41654.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|EMBL:AAC41654.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP AND INDUCTION.
RC STRAIN=cv. Castlemart {ECO:0000312|EMBL:AAC41654.1};
RC TISSUE=Fruit {ECO:0000312|EMBL:AAC41654.1};
RX PubMed=7784511; DOI=10.1104/pp.108.1.411;
RA Grantz A.A., Brummell D.A., Bennett A.B.;
RT "Ascorbate free radical reductase mRNA levels are induced by wounding.";
RL Plant Physiol. 108:411-418(1995).
CC -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to
CC ascorbate, oxidizing NADH in the process.
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:7784511};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9S926,
CC ECO:0000255|RuleBase:RU000401};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, and to a lesser degree in
CC stems, roots and all stages of fruit. {ECO:0000269|PubMed:7784511}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:7784511}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; L41345; AAC41654.1; -; Genomic_DNA.
DR PIR; T06407; T06407.
DR AlphaFoldDB; Q43497; -.
DR SMR; Q43497; -.
DR STRING; 4081.Solyc09g009390.2.1; -.
DR PaxDb; Q43497; -.
DR PRIDE; Q43497; -.
DR ProMEX; Q43497; -.
DR eggNOG; KOG1336; Eukaryota.
DR InParanoid; Q43497; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; Q43497; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0098869; P:cellular oxidant detoxification; 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.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..433
FT /note="Monodehydroascorbate reductase"
FT /id="PRO_0000209142"
FT BINDING 13..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 52
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 146..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 171..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 173..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 313..314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 313..314
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 319
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 348
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 348
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 350
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
SQ SEQUENCE 433 AA; 47036 MW; 6E3375DB73A1391A CRC64;
MAEKSFKYVI VGGGVSAGYA AREFAKQGVK PGELAIISKE AVAPYERPAL SKAYLFPEGA
ARLPGFHVCV GSGGERQLPE WYAEKGISLI LSTEIVKADL ASKTLVSAAG ESFKYQTLVI
ATGTTVLKLS DFGVQGADSK NIFYLREIDD ADQLVEALKA KKNGKAVVVG GGYIGLELSA
VLRLNNIEVN MVYPEPWCMP RLFTEGIAAF YEGYYKNKGV NIIKGTVAVG FDTHPNGEVK
EVKLKDGRVL EADIVVVGVG ARPLTTLFKG QVEEEKGGIK TDAFFKTSVP DVYAVGDVAT
FPLKMYNEIR RVEHVDHSRK SAEQAVKAIF ASEQGKSVDE YDYLPYFYSR AFDLSWQFYG
DNVGETVLFG DADPNSATHK FGQYWIKDGK IVGAFLESGS PEENKAIAKV AKVQPPATLD
QLAQEGISFA SKI
