ID   MDAR2_SOYBN             Reviewed;          10 AA.
AC   Q9S926;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Monodehydroascorbate reductase II;
DE            Short=MDARII;
DE            Short=MRII;
DE            EC=1.6.5.4;
DE   AltName: Full=Ascorbate free radical reductase II;
DE            Short=AFR reductase II;
DE   Flags: Fragment;
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=cv. Williams {ECO:0000269|PubMed:1727643};
RC   TISSUE=Root nodule {ECO:0000269|PubMed:1727643};
RX   PubMed=1727643; DOI=10.1016/0003-9861(92)90080-g;
RA   Dalton D.A., Langeberg L., Robbins M.;
RT   "Purification and characterization of monodehydroascorbate reductase from
RT   soybean root nodules.";
RL   Arch. Biochem. Biophys. 292:281-286(1992).
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:1727643};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:1727643};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.6 uM for NADH;
CC         KM=150 uM for NADPH;
CC         KM=7 uM for monodehydroascorbate;
CC         Vmax=288 umol/min/mg enzyme for NADH oxidation reaction;
CC       pH dependence:
CC         Optimum pH is 8.0-9.0.;
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   PIR; A44871; A44871.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           <1..>10
FT                   /note="Monodehydroascorbate reductase II"
FT                   /id="PRO_0000209144"
FT   BINDING         5..>10
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:1727643"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:1727643"
SQ   SEQUENCE   10 AA;  1153 MW;  848025504B5339D1 CRC64;
     AKTFKYIILG