FQRL2_ARATH
ID FQRL2_ARATH Reviewed; 273 AA.
AC O23207; Q8LB59;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable NAD(P)H dehydrogenase (quinone) FQR1-like 2 {ECO:0000305};
DE EC=1.6.5.2 {ECO:0000250|UniProtKB:Q9LSQ5};
GN OrderedLocusNames=At4g36750 {ECO:0000312|Araport:AT4G36750};
GN ORFNames=C7A10.610 {ECO:0000312|EMBL:CAB16805.1};
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;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Catalyzes the transfer of electrons from NADH and NADPH to
CC reduce quinone to the hydroquinone state.
CC {ECO:0000250|UniProtKB:Q9LSQ5}.
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:0000250|UniProtKB:Q9LSQ5};
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:0000250|UniProtKB:Q9LSQ5};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9LSQ5};
CC Note=Binds 1 FMN per monomer. {ECO:0000250|UniProtKB:Q9LSQ5};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; Z99708; CAB16805.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80341.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86697.1; -; Genomic_DNA.
DR EMBL; AY087410; AAM64959.1; -; mRNA.
DR PIR; A85434; A85434.
DR RefSeq; NP_195393.1; NM_119839.6.
DR AlphaFoldDB; O23207; -.
DR SMR; O23207; -.
DR BioGRID; 15109; 3.
DR STRING; 3702.AT4G36750.1; -.
DR iPTMnet; O23207; -.
DR SwissPalm; O23207; -.
DR PaxDb; O23207; -.
DR PRIDE; O23207; -.
DR ProteomicsDB; 230042; -.
DR EnsemblPlants; AT4G36750.1; AT4G36750.1; AT4G36750.
DR GeneID; 829828; -.
DR Gramene; AT4G36750.1; AT4G36750.1; AT4G36750.
DR KEGG; ath:AT4G36750; -.
DR Araport; AT4G36750; -.
DR TAIR; locus:2115405; AT4G36750.
DR eggNOG; KOG3135; Eukaryota.
DR HOGENOM; CLU_051402_0_1_1; -.
DR InParanoid; O23207; -.
DR OMA; HGMLIMG; -.
DR OrthoDB; 1312785at2759; -.
DR PhylomeDB; O23207; -.
DR BioCyc; ARA:AT4G36750-MON; -.
DR PRO; PR:O23207; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23207; baseline and differential.
DR Genevisible; O23207; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; 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 Cell membrane; Flavoprotein; FMN; Membrane; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..273
FT /note="Probable NAD(P)H dehydrogenase (quinone) FQR1-like
FT 2"
FT /id="PRO_0000431285"
FT DOMAIN 75..263
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
FT BINDING 183..236
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 207
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
FT CONFLICT 55
FT /note="G -> A (in Ref. 4; AAM64959)"
SQ SEQUENCE 273 AA; 28754 MW; 56DBACF13152DFC2 CRC64;
MGKGGGCVPS KKKKPATTGD GPGIDDDNDA TNAPIQIDDD QTTIDGDRTT ATNTGGTTTP
AITTTAAKIS SPLKIFVVFY SMYGHVESLA KRMKKGVDSV EGVEATLYRV PETLSQEVVE
QMKAPVKDLE IPEITAAELT AADGFLFGFP TRYGCMAAQM KAFFDSTGSL WKEQSLAGKP
AGFFVSTGTQ GGGQETTAWT AITQLVHHGM LFVPIGYTFG AGMFKMDSIR GGSPYGAGVF
AGDGSREATE TELALAEHQG NYMAAIVKRL AQP
