FQRL3_ARATH
ID FQRL3_ARATH Reviewed; 207 AA.
AC Q9LUX9;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable NAD(P)H dehydrogenase (quinone) FQR1-like 3 {ECO:0000305};
DE EC=1.6.5.2 {ECO:0000250|UniProtKB:Q9LSQ5};
GN OrderedLocusNames=At5g58800 {ECO:0000312|Araport:AT5G58800};
GN ORFNames=MZN1.26 {ECO:0000312|EMBL:BAA97350.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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).
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 -!- INTERACTION:
CC Q9LUX9; Q8L746: NPR3; NbExp=3; IntAct=EBI-4445291, EBI-4441365;
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; AB020755; BAA97350.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97105.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97106.1; -; Genomic_DNA.
DR EMBL; AY064055; AAL36411.1; -; mRNA.
DR EMBL; AY096367; AAM20008.1; -; mRNA.
DR RefSeq; NP_001032099.1; NM_001037022.1.
DR RefSeq; NP_200688.2; NM_125270.5.
DR AlphaFoldDB; Q9LUX9; -.
DR SMR; Q9LUX9; -.
DR BioGRID; 21241; 2.
DR IntAct; Q9LUX9; 2.
DR STRING; 3702.AT5G58800.2; -.
DR PaxDb; Q9LUX9; -.
DR PRIDE; Q9LUX9; -.
DR ProteomicsDB; 230017; -.
DR EnsemblPlants; AT5G58800.1; AT5G58800.1; AT5G58800.
DR EnsemblPlants; AT5G58800.2; AT5G58800.2; AT5G58800.
DR GeneID; 835997; -.
DR Gramene; AT5G58800.1; AT5G58800.1; AT5G58800.
DR Gramene; AT5G58800.2; AT5G58800.2; AT5G58800.
DR KEGG; ath:AT5G58800; -.
DR Araport; AT5G58800; -.
DR TAIR; locus:2178868; AT5G58800.
DR eggNOG; KOG3135; Eukaryota.
DR HOGENOM; CLU_051402_0_1_1; -.
DR InParanoid; Q9LUX9; -.
DR OMA; SRFGMMA; -.
DR OrthoDB; 1312785at2759; -.
DR PhylomeDB; Q9LUX9; -.
DR BioCyc; ARA:AT5G58800-MON; -.
DR PRO; PR:Q9LUX9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LUX9; baseline and differential.
DR Genevisible; Q9LUX9; AT.
DR GO; GO:0009536; C:plastid; 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 Flavoprotein; FMN; NAD; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..207
FT /note="Probable NAD(P)H dehydrogenase (quinone) FQR1-like
FT 3"
FT /id="PRO_0000431286"
FT DOMAIN 6..194
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 12..16
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
FT BINDING 114..167
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 138
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
SQ SEQUENCE 207 AA; 22723 MW; A351D6F7E40FB384 CRC64;
MAVTKIYIVY YSLHGHVETM AREVLRGVNS VPDVEATLWQ VPETLPEKIL EKVKAVPRPD
DVPDIRPEQL AEADGFMFGF PSRFGVMASQ VMTFFDNTND LWTTQALAGK PAGIFWSTGF
HGGGQELTAL TAVTKLAHHG MIFVPVGYTF GKSMYEMGEV KGGSPYGSGT YAADGSREPT
ELEIQQANYH GKYFAGIAKK LKKRSPV
