ID   NQR_ARATH               Reviewed;         196 AA.
AC   Q9LK88; Q9XFI5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=NADPH:quinone oxidoreductase;
DE            EC=1.6.5.2;
GN   Name=NQR; OrderedLocusNames=At3g27890; ORFNames=K16N12.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX   PubMed=10606758; DOI=10.1016/s0014-5793(99)01625-7;
RA   Sparla F., Tedeschi G., Pupillo P., Trost P.;
RT   "Cloning and heterologous expression of NAD(P)H:quinone reductase of
RT   Arabidopsis thaliana, a functional homologue of animal DT-diaphorase.";
RL   FEBS Lett. 463:382-386(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA   Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA   Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT   "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT   proteome.";
RL   Mol. Cell. Proteomics 3:675-691(2004).
CC   -!- FUNCTION: The enzyme apparently serves as a quinone reductase in
CC       connection with conjugation reactions of hydroquinones involved in
CC       detoxification pathways.
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:0000269|PubMed:10606758};
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:0000269|PubMed:10606758};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:10606758};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10606758}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC   -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR   EMBL; AF145234; AAD37373.1; -; mRNA.
DR   EMBL; AP000371; BAB02535.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77376.1; -; Genomic_DNA.
DR   RefSeq; NP_189427.1; NM_113705.4.
DR   AlphaFoldDB; Q9LK88; -.
DR   SMR; Q9LK88; -.
DR   STRING; 3702.AT3G27890.1; -.
DR   iPTMnet; Q9LK88; -.
DR   PaxDb; Q9LK88; -.
DR   PRIDE; Q9LK88; -.
DR   ProteomicsDB; 239054; -.
DR   EnsemblPlants; AT3G27890.1; AT3G27890.1; AT3G27890.
DR   GeneID; 822411; -.
DR   Gramene; AT3G27890.1; AT3G27890.1; AT3G27890.
DR   KEGG; ath:AT3G27890; -.
DR   Araport; AT3G27890; -.
DR   TAIR; locus:2086445; AT3G27890.
DR   eggNOG; KOG4530; Eukaryota.
DR   HOGENOM; CLU_055322_4_2_1; -.
DR   InParanoid; Q9LK88; -.
DR   OMA; YGGVWAQ; -.
DR   OrthoDB; 1223874at2759; -.
DR   PhylomeDB; Q9LK88; -.
DR   BioCyc; ARA:AT3G27890-MON; -.
DR   BRENDA; 1.6.5.2; 399.
DR   BRENDA; 7.1.1.2; 399.
DR   PRO; PR:Q9LK88; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LK88; baseline and differential.
DR   Genevisible; Q9LK88; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005025; FMN_Rdtase-like.
DR   Pfam; PF03358; FMN_red; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Flavoprotein; FMN; Membrane; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..196
FT                   /note="NADPH:quinone oxidoreductase"
FT                   /id="PRO_0000160601"
FT   CONFLICT        178
FT                   /note="R -> K (in Ref. 1; AAD37373)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   196 AA;  21556 MW;  FE74952BC1CB2C18 CRC64;
     MEAVTAIKPL IRVAALSGSL RKTSFHTGLL RAAIDLTKES VPGLQIEYID ISPLPLINTD
     LEVNGTYPPV VEAFRQKILE ADSILFASPE YNFSVSAPLK NALDWASRPP NVWADKPAAI
     ISTGGGFGGG RSQYHLRQIG VFLDLHFINK PEFTLNAFQP PQKFDAEGNL VDEVTKERLK
     QVLLSLQAFT LRLQGK