MDAR_PEA
ID MDAR_PEA Reviewed; 433 AA.
AC Q40977;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
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;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888 {ECO:0000312|EMBL:AAA60979.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Leaf {ECO:0000269|PubMed:7983054};
RX PubMed=7983054; DOI=10.1016/s0021-9258(18)47399-1;
RA Murthy S.S., Zilinskas B.A.;
RT "Molecular cloning and characterization of a cDNA encoding pea
RT monodehydroascorbate reductase.";
RL J. Biol. Chem. 269:31129-31133(1994).
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:7983054};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9S926,
CC ECO:0000255|RuleBase:RU000401};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 uM for NADH;
CC KM=21.5 uM for NADPH;
CC KM=5.7 uM for monodehydroascorbate;
CC Vmax=312 umol/min/mg enzyme for NADH oxidation reaction;
CC Vmax=40.9 umol/min/mg enzyme for NADPH oxidation reaction;
CC pH dependence:
CC Optimum pH is 7.5-9.5.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at relatively low levels in all tissues
CC examined. {ECO:0000269|PubMed:7983054}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; U06461; AAA60979.1; -; mRNA.
DR PIR; A55333; A55333.
DR AlphaFoldDB; Q40977; -.
DR SMR; Q40977; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:UniProtKB-EC.
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.
FT CHAIN 1..433
FT /note="Monodehydroascorbate reductase"
FT /id="PRO_0000209143"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 145..146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 170..176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 172..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 312..313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 312..313
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 318
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 347
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 349
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
SQ SEQUENCE 433 AA; 47309 MW; 5435C1F9E2BFCC97 CRC64;
MVHSFKYIII GGGVSAGYAA REFVKQGVHP GELAIISKEA VAPYERPALS KAYLFPESPA
RLPGFHTCVG SGGERLLPEW YSEKGIQLYL STEIVSADLA AKFLKSANGE HFDYQTLVIA
TGSAVIRLTD FGVIGANAKN IFYLREVDDA DKLYEAIKRK KNAKRVVVGG GYIGLELSAV
LKLNDLDVTM VYPEPWCMPR LFTSEIAAFY EGYYANKGIN IIKGTVAVGF TANSDGEVKE
VKLKDGRVLE ADIVIVGVGG RPQISLFKGQ VEEQHGGIKT DSFFKTSVPD VYAVGDVATF
PLKLYNDVRR VEHVDHARKS AEQAAKAIFA ADVGKSVEEY DYLPYFYSRS FDLSWQFYGD
NVGETVLFGD NDPASSKPKF GTYWIKEGKV VGAFLEGGTP DENKAIAKVA RAKPAVEDVN
QLAEEGLSFA SKI
