FQR1_ARATH
ID FQR1_ARATH Reviewed; 204 AA.
AC Q9LSQ5;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=NAD(P)H dehydrogenase (quinone) FQR1 {ECO:0000305};
DE EC=1.6.5.2 {ECO:0000269|PubMed:11842161};
DE AltName: Full=Flavodoxin-like quinone reductase 1 {ECO:0000303|PubMed:11842161};
GN Name=FQR1 {ECO:0000303|PubMed:11842161};
GN OrderedLocusNames=At5g54500 {ECO:0000312|Araport:AT5G54500};
GN ORFNames=F24B18.12 {ECO:0000312|EMBL:BAA97523.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION BY AUXIN.
RX PubMed=11842161; DOI=10.1104/pp.010581;
RA Laskowski M.J., Dreher K.A., Gehring M.A., Abel S., Gensler A.L.,
RA Sussex I.M.;
RT "FQR1, a novel primary auxin-response gene, encodes a flavin
RT mononucleotide-binding quinone reductase.";
RL Plant Physiol. 128:578-590(2002).
RN [5]
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).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=23464356; DOI=10.1111/ppl.12042;
RA Heyno E., Alkan N., Fluhr R.;
RT "A dual role for plant quinone reductases in host-fungus interaction.";
RL Physiol. Plantarum 149:340-353(2013).
CC -!- FUNCTION: Catalyzes the transfer of electrons from NADH and NADPH to
CC several quinones in vitro. May act as detoxification enzyme, and
CC protect against auxin-induced oxidative stress.
CC {ECO:0000269|PubMed:11842161}.
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:11842161};
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:11842161};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000305|PubMed:11842161};
CC Note=Binds 1 FMN per monomer. {ECO:0000305|PubMed:11842161};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LSQ5-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased resistance to the
CC necrotrophic fungus Botrytis cinerea. {ECO:0000269|PubMed:23464356}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; AB026634; BAA97523.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96502.1; -; Genomic_DNA.
DR EMBL; AY120735; AAM53293.1; -; mRNA.
DR EMBL; BT002194; AAN72205.1; -; mRNA.
DR RefSeq; NP_200261.1; NM_124830.6. [Q9LSQ5-1]
DR AlphaFoldDB; Q9LSQ5; -.
DR SMR; Q9LSQ5; -.
DR iPTMnet; Q9LSQ5; -.
DR PRIDE; Q9LSQ5; -.
DR ProMEX; Q9LSQ5; -.
DR ProteomicsDB; 230560; -. [Q9LSQ5-1]
DR EnsemblPlants; AT5G54500.1; AT5G54500.1; AT5G54500. [Q9LSQ5-1]
DR GeneID; 835538; -.
DR Gramene; AT5G54500.1; AT5G54500.1; AT5G54500. [Q9LSQ5-1]
DR KEGG; ath:AT5G54500; -.
DR Araport; AT5G54500; -.
DR HOGENOM; CLU_051402_0_1_1; -.
DR OMA; LHFGMVI; -.
DR PhylomeDB; Q9LSQ5; -.
DR BioCyc; ARA:AT5G54500-MON; -.
DR PRO; PR:Q9LSQ5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSQ5; baseline and differential.
DR Genevisible; Q9LSQ5; AT.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:UniProtKB.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0071365; P:cellular response to auxin stimulus; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR010089; Flavoprotein_WrbA-like.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01755; flav_wrbA; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Flavoprotein; FMN; Membrane; NAD;
KW NADP; Nucleotide-binding; Oxidoreductase; Reference proteome;
KW Stress response.
FT CHAIN 1..204
FT /note="NAD(P)H dehydrogenase (quinone) FQR1"
FT /id="PRO_0000431283"
FT DOMAIN 5..192
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 11..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
FT BINDING 112..165
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
SQ SEQUENCE 204 AA; 21796 MW; 0928B6DA346A3E6B CRC64;
MATKVYIVYY SMYGHVEKLA EEIRKGAASV EGVEAKLWQV PETLHEEALS KMSAPPKSES
PIITPNELAE ADGFVFGFPT RFGMMAAQFK AFLDATGGLW RAQALAGKPA GIFYSTGSQG
GGQETTALTA ITQLVHHGML FVPIGYTFGA GMFEMENVKG GSPYGAGTFA GDGSRQPTEL
ELQQAFHQGQ YIASITKKLK GSTA
