ID A0A3B6QH25_WHEAT Unreviewed; 476 AA.
AC A0A3B6QH25;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=monodehydroascorbate reductase (NADH) {ECO:0000256|ARBA:ARBA00038920};
DE EC=1.6.5.4 {ECO:0000256|ARBA:ARBA00038920};
GN ORFNames=CFC21_093347 {ECO:0000313|EMBL:KAF7090623.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6D02G254000.1};
RN [1] {ECO:0000313|EMBL:KAF7090623.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7090623.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6D02G254000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6D02G254000.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6D02G254000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7090623.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7090623.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00036831};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; CM022228; KAF7090623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6QH25; -.
DR SMR; A0A3B6QH25; -.
DR STRING; 4565.A0A3B6QH25; -.
DR EnsemblPlants; TraesCS6D02G254000.1; TraesCS6D02G254000.1; TraesCS6D02G254000.
DR Gramene; TraesCAD_scaffold_034015_01G000300.1; TraesCAD_scaffold_034015_01G000300.1; TraesCAD_scaffold_034015_01G000300.
DR Gramene; TraesCLE_scaffold_071447_01G000100.1; TraesCLE_scaffold_071447_01G000100.1; TraesCLE_scaffold_071447_01G000100.
DR Gramene; TraesCS6D02G254000.1; TraesCS6D02G254000.1; TraesCS6D02G254000.
DR Gramene; TraesCS6D03G0612800.1; TraesCS6D03G0612800.1.CDS; TraesCS6D03G0612800.
DR Gramene; TraesKAR6D01G0272640.1; cds.TraesKAR6D01G0272640.1; TraesKAR6D01G0272640.
DR Gramene; TraesPAR_scaffold_032234_01G000100.1; TraesPAR_scaffold_032234_01G000100.1; TraesPAR_scaffold_032234_01G000100.
DR Gramene; TraesRN6D0100648600.1; TraesRN6D0100648600.1; TraesRN6D0100648600.
DR Gramene; TraesROB_scaffold_026869_01G000100.1; TraesROB_scaffold_026869_01G000100.1; TraesROB_scaffold_026869_01G000100.
DR Gramene; TraesWEE_scaffold_031142_01G000300.1; TraesWEE_scaffold_031142_01G000300.1; TraesWEE_scaffold_031142_01G000300.
DR OMA; MFRPEKF; -.
DR OrthoDB; 804at2759; -.
DR Proteomes; UP000019116; Chromosome 6D.
DR Proteomes; UP000815260; Chromosome 6D.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 InterPro; IPR048618; MDHAR3-like_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF21791; MDHAR3-like_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..322
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 342..427
FT /note="Monodehydroascorbate reductase 3-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21791"
SQ SEQUENCE 476 AA; 52079 MW; 5005109243126DF9 CRC64;
MGRAFVYVVL GGGVAAGYAA LEFARRGGYS RGELCIISEE AVAPYERPAL SKGYLLPEDP
SRLPKFHTCV GANDELLTTK WYKEQGIELV LGTRVISADV RRKTLLTATG ETISYKTLII
ATGARALKLE EFGISGSDAA NICYLRNLED ADKLVNAMSS CSGGNAVVIG GGYIGMECAA
ALVTNKIKVT MVFPEKHCMG RLFTEKIAEY YESYYTSKGV TFTKGTVLTS FEKDSTGKVT
SVVLRDGNHL PADMVVVGIG IRANTSLFEG QLLMEKGGIK VNGQMQTSDS SVYAVGDVAA
FPIKLFDGDI RRLEHVDSAR RTARHAVAAI LEPSKTRDVD YLPFFYSRVF TLSWQFYGDN
VGEVIHYGDF TSNSPMFGAY WVSKGQITGA FLEGGNRDDY EALSVVVRRK TKVSDMPELE
RQGLAFAIQE SKKDVPDSGV TLGEKPTFVW YATAGVVAAV SISAFGYWYG RKRRRW
//