MDARF_CUCSA
ID MDARF_CUCSA Reviewed; 166 AA.
AC P83966;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Monodehydroascorbate reductase, fruit isozyme;
DE Short=MDAR fruit;
DE EC=1.6.5.4;
DE AltName: Full=Ascorbate free radical reductase fruit;
DE Short=AFR reductase fruit;
DE Flags: Fragments;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Fruit {ECO:0000269|PubMed:8055175};
RX PubMed=8055175;
RA Sano S., Asada K.;
RT "cDNA cloning of monodehydroascorbate radical reductase from Cucumber: a
RT high degree of homology in terms of amino acid sequence between this enzyme
RT and bacterial flavoenzymes.";
RL Plant Cell Physiol. 35:425-437(1994).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Fruit {ECO:0000269|PubMed:4055727};
RX PubMed=4055727; DOI=10.1016/s0021-9258(17)38813-0;
RA Hossain M.A., Asada K.;
RT "Monodehydroascorbate reductase from cucumber is a flavin adenine
RT dinucleotide enzyme.";
RL J. Biol. Chem. 260:12920-12926(1985).
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:4055727};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:4055727};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 uM for NADH;
CC KM=23 uM for NADPH;
CC KM=1.4 uM for monodehydroascorbate;
CC Vmax=256 umol/min/mg enzyme for NADH oxidation reaction;
CC Vmax=192 umol/min/mg enzyme for NADPH oxidation reaction;
CC pH dependence:
CC Optimum pH is 7-9.;
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8055175}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P83966; -.
DR SMR; P83966; -.
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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Redox-active center.
FT CHAIN <1..>166
FT /note="Monodehydroascorbate reductase, fruit isozyme"
FT /id="PRO_0000209141"
FT UNSURE 92
FT /note="L or K"
FT NON_CONS 13..14
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_CONS 32..33
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_CONS 58..59
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_CONS 92..93
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_CONS 128..129
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_CONS 135..136
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_CONS 150..151
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:8055175"
FT NON_TER 166
FT /evidence="ECO:0000303|PubMed:8055175"
SQ SEQUENCE 166 AA; 18811 MW; 0816E13BF68A6260 CRC64;
EAVAPYERPA LSKNIFYLRE IADADQLVEA IKLKDGRTLD ADIVVVGVGG RPLVSLFKTS
IPDVYAVGDV ATYPLKLYNE LRRVEHVDHA RLSIEEYDYL PYFYSRTFNL AWQFYGDNVG
ETVLFPDNFG TYWIKVVGVF LEGGTPDEYK VARVQPPVES LDQLAK
