ID M5X5F6_PRUPE Unreviewed; 235 AA.
AC M5X5F6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000256|ARBA:ARBA00012648};
DE EC=1.6.5.2 {ECO:0000256|ARBA:ARBA00012648};
GN ORFNames=PRUPE_2G038000 {ECO:0000313|EMBL:ONI20870.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI20870.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI20870.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000139};
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DR EMBL; CM007652; ONI20870.1; -; Genomic_DNA.
DR RefSeq; XP_007220093.1; XM_007220031.1.
DR AlphaFoldDB; M5X5F6; -.
DR STRING; 3760.M5X5F6; -.
DR EnsemblPlants; ONI20870; ONI20870; PRUPE_2G038000.
DR GeneID; 18787064; -.
DR Gramene; ONI20870; ONI20870; PRUPE_2G038000.
DR KEGG; pper:18787064; -.
DR eggNOG; KOG4530; Eukaryota.
DR HOGENOM; CLU_055322_4_2_1; -.
DR OMA; NSKCESH; -.
DR OrthoDB; 73508at2759; -.
DR Proteomes; UP000006882; Chromosome g2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR PANTHER; PTHR30543; CHROMATE REDUCTASE; 1.
DR PANTHER; PTHR30543:SF21; NAD(P)H-DEPENDENT FMN REDUCTASE LOT6; 1.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006882}.
FT DOMAIN 50..196
FT /note="NADPH-dependent FMN reductase-like"
FT /evidence="ECO:0000259|Pfam:PF03358"
SQ SEQUENCE 235 AA; 25860 MW; 80DFE151FAAFAF92 CRC64;
MEEEDSSVAA KSVVKVEVGL GQLCRCFCLF GTRAAPITNK SKNINKNSVI KVAAVCGSLR
EASYNRCLIR SAIEISKTSI DGLEIEYVDI SALPFLNVDL EGKDGSFPPA VEAFRRKILE
ADSILFASPE YNYSISAPLK NAIDWASRPP NAWADKAAAV VSASGDFGGG RSQYHLRQVG
VSLDLHFINK PEFFLDGLKS PEKFDSRNLV DEQDKERLKE ILLALQAFTL RLQTK
//
