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 30-AUG-2017, entry version 113. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 RP SCALE 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 RT membrane 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 RT interaction."; RL Physiol. Plantarum 149:340-353(2013). CC -!- FUNCTION: Catalyzes the transfer of electrons from NADH and NADPH CC to several quinones in vitro. May act as detoxification enzyme, CC and protect against auxin-induced oxidative stress. CC {ECO:0000269|PubMed:11842161}. CC -!- CATALYTIC ACTIVITY: NAD(P)H + a quinone = NAD(P)(+) + a CC hydroquinone. {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. CC {ECO:0000269|PubMed:23464356}. CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; At.43051; -. DR ProteinModelPortal; Q9LSQ5; -. DR SMR; Q9LSQ5; -. DR iPTMnet; Q9LSQ5; -. DR PRIDE; Q9LSQ5; -. DR ProMEX; Q9LSQ5; -. DR EnsemblPlants; AT5G54500.1; AT5G54500.1; AT5G54500. [Q9LSQ5-1] DR GeneID; 835538; -. DR Gramene; AT5G54500.1; AT5G54500.1; AT5G54500. DR KEGG; ath:AT5G54500; -. DR Araport; AT5G54500; -. DR HOGENOM; HOG000030539; -. DR InParanoid; Q9LSQ5; -. DR PhylomeDB; Q9LSQ5; -. DR BioCyc; ARA:AT5G54500-MONOMER; -. 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:0071365; P:cellular response to auxin stimulus; IDA:UniProtKB. DR GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_01017; NQOR; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_dom. 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; Complete proteome; Flavoprotein; KW FMN; Membrane; NAD; NADP; Nucleotide-binding; Oxidoreductase; KW Reference proteome; Stress response. FT CHAIN 1 204 NAD(P)H dehydrogenase (quinone) FQR1. FT /FTId=PRO_0000431283. FT DOMAIN 5 192 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. FT NP_BIND 11 15 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. FT NP_BIND 112 165 FMN. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. FT BINDING 13 13 NAD. {ECO:0000250|UniProtKB:P0A8G6}. FT BINDING 136 136 FMN. {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 //