FNRL1_ARATH
ID FNRL1_ARATH Reviewed; 360 AA.
AC Q9FKW6; Q0WWE2; Q9SUJ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic;
DE EC=1.18.1.2 {ECO:0000269|Ref.7};
DE AltName: Full=Leaf FNR 1 {ECO:0000303|Ref.7};
DE Short=AtLFNR1 {ECO:0000303|Ref.7};
DE Short=FNR-1 {ECO:0000303|Ref.7};
DE Flags: Precursor;
GN Name=LFNR1 {ECO:0000303|Ref.7}; Synonyms=PETH1;
GN OrderedLocusNames=At5g66190 {ECO:0000312|Araport:AT5G66190};
GN ORFNames=K2A18.27 {ECO:0000312|EMBL:BAB10424.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Legen J., Misera S., Herrmann R.G., Altschmied L.;
RT "Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding
RT organellar polypeptides.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY NITRATE.
RX PubMed=10948265; DOI=10.2307/3871145;
RA Wang R., Guegler K., LaBrie S.T., Crawford N.M.;
RT "Genomic analysis of a nutrient response in Arabidopsis reveals diverse
RT expression patterns and novel metabolic and potential regulatory genes
RT induced by nitrate.";
RL Plant Cell 12:1491-1509(2000).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, PROTEIN SEQUENCE OF 50-59, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX DOI=10.1111/j.1365-3040.2005.01352.x;
RA Hanke G.T., Okutani S., Satomi Y., Takao T., Suzuki A., Hase T.;
RT "Multiple iso-proteins of FNR in Arabidopsis: evidence for different
RT contributions to chloroplast function and nitrogen assimilation.";
RL Plant Cell Environ. 28:1146-1157(2005).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17335513; DOI=10.1111/j.1365-313x.2006.03014.x;
RA Lintala M., Allahverdiyeva Y., Kidron H., Piippo M., Battchikova N.,
RA Suorsa M., Rintamaeki E., Salminen T.A., Aro E.-M., Mulo P.;
RT "Structural and functional characterization of ferredoxin-NADP+-
RT oxidoreductase using knock-out mutants of Arabidopsis.";
RL Plant J. 49:1041-1052(2007).
RN [9]
RP INTERACTION WITH PGRL1A AND PGRL1B.
RC STRAIN=cv. Columbia;
RX PubMed=18243102; DOI=10.1016/j.cell.2007.12.028;
RA DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D.,
RA Finazzi G., Joliot P., Barbato R., Leister D.;
RT "A complex containing PGRL1 and PGR5 is involved in the switch between
RT linear and cyclic electron flow in Arabidopsis.";
RL Cell 132:273-285(2008).
RN [10]
RP INTERACTION WITH TIC62.
RX PubMed=20040542; DOI=10.1105/tpc.109.069815;
RA Benz J.P., Stengel A., Lintala M., Lee Y.H., Weber A., Philippar K.,
RA Guegel I.L., Kaieda S., Ikegami T., Mulo P., Soll J., Boelter B.;
RT "Arabidopsis Tic62 and ferredoxin-NADP(H) oxidoreductase form light-
RT regulated complexes that are integrated into the chloroplast redox poise.";
RL Plant Cell 21:3965-3983(2009).
RN [11]
RP INTERACTION WITH TIC62.
RX PubMed=20934402; DOI=10.1016/j.bbabio.2010.10.001;
RA Mulo P.;
RT "Chloroplast-targeted ferredoxin-NADP(+) oxidoreductase (FNR): structure,
RT function and location.";
RL Biochim. Biophys. Acta 1807:927-934(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND THR-210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [13]
RP DISULFIDE BOND.
RX PubMed=26941088; DOI=10.1105/tpc.15.01027;
RA Yang C., Hu H., Ren H., Kong Y., Lin H., Guo J., Wang L., He Y., Ding X.,
RA Grabsztunowicz M., Mulo P., Chen T., Liu Y., Wu Z., Wu Y., Mao C., Wu P.,
RA Mo X.;
RT "LIGHT-INDUCED RICE1 regulates light-dependent attachment of LEAF-TYPE
RT FERREDOXIN-NADP+ OXIDOREDUCTASE to the thylakoid membrane in rice and
RT Arabidopsis.";
RL Plant Cell 28:712-728(2016).
CC -!- FUNCTION: Plays a key role in regulating the relative amounts of cyclic
CC and non-cyclic electron flow to meet the demands of the plant for ATP
CC and reducing power. {ECO:0000269|PubMed:17335513, ECO:0000269|Ref.7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2; Evidence={ECO:0000269|Ref.7};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 uM for ferredoxin-1 {ECO:0000269|Ref.7};
CC KM=2.5 uM for ferredoxin-2 {ECO:0000269|Ref.7};
CC KM=4.6 uM for ferredoxin-3 {ECO:0000269|Ref.7};
CC -!- PATHWAY: Energy metabolism; photosynthesis. {ECO:0000269|Ref.7}.
CC -!- SUBUNIT: Heterodimer with LFNR2. Interacts with PGRL1A and PGRL1B.
CC Interacts with TIC62. Component of high molecular weight thylakoid
CC LFNRs-containing protein complexes containing LIR1, LFNR1, LFNR2, TIC62
CC and TROL proteins. Interacts directly with LIR1 and TIC62; LIR1
CC increases the affinity of LFNR1 and LFNR2 for TIC62 (By similarity).
CC {ECO:0000250|UniProtKB:P41344, ECO:0000269|PubMed:17335513,
CC ECO:0000269|PubMed:18243102, ECO:0000269|PubMed:20040542,
CC ECO:0000269|PubMed:20934402}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|Ref.7}.
CC Plastid, chloroplast thylakoid membrane {ECO:0000269|Ref.7}; Peripheral
CC membrane protein {ECO:0000269|Ref.7}; Stromal side {ECO:0000269|Ref.7}.
CC Note=More abundant in the membrane fraction. {ECO:0000269|Ref.7}.
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=Q9FKW6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoots. Restricted to green tissues,
CC being more abundant in siliques. {ECO:0000269|Ref.7}.
CC -!- INDUCTION: By nitrate. {ECO:0000269|PubMed:10948265}.
CC -!- PTM: May form interchain disulfide bonds with LIR1.
CC {ECO:0000269|PubMed:26941088}.
CC -!- DISRUPTION PHENOTYPE: Plants have a reduced capacity for carbon
CC fixation and prevent the association of LFNR2 with the thylakoid
CC membrane. {ECO:0000269|PubMed:17335513}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AJ243705; CAB52472.1; -; mRNA.
DR EMBL; AB011474; BAB10424.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98174.1; -; Genomic_DNA.
DR EMBL; AY072112; AAL59934.1; -; mRNA.
DR EMBL; AY096665; AAM20299.1; -; mRNA.
DR EMBL; AK226411; BAE98556.1; -; mRNA.
DR RefSeq; NP_201420.1; NM_126017.5. [Q9FKW6-1]
DR AlphaFoldDB; Q9FKW6; -.
DR SMR; Q9FKW6; -.
DR BioGRID; 21993; 8.
DR IntAct; Q9FKW6; 1.
DR STRING; 3702.AT5G66190.1; -.
DR iPTMnet; Q9FKW6; -.
DR PaxDb; Q9FKW6; -.
DR PRIDE; Q9FKW6; -.
DR ProteomicsDB; 230434; -. [Q9FKW6-1]
DR EnsemblPlants; AT5G66190.1; AT5G66190.1; AT5G66190. [Q9FKW6-1]
DR GeneID; 836751; -.
DR Gramene; AT5G66190.1; AT5G66190.1; AT5G66190. [Q9FKW6-1]
DR KEGG; ath:AT5G66190; -.
DR Araport; AT5G66190; -.
DR TAIR; locus:2156917; AT5G66190.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; Q9FKW6; -.
DR OMA; CYREACV; -.
DR OrthoDB; 817123at2759; -.
DR PhylomeDB; Q9FKW6; -.
DR BioCyc; ARA:AT5G66190-MON; -.
DR BRENDA; 1.18.1.2; 399.
DR UniPathway; UPA00091; -.
DR PRO; PR:Q9FKW6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKW6; baseline and differential.
DR Genevisible; Q9FKW6; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; ISS:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IDA:TAIR.
DR GO; GO:0045157; F:electron transporter, transferring electrons within the noncyclic electron transport pathway of photosynthesis activity; IDA:TAIR.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR015701; FNR.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR035442; FNR_plant_Cyanobacteria.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43314; PTHR43314; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF501178; FNR-PetH; 1.
DR PIRSF; PIRSF000361; Frd-NADP+_RD; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing;
KW Disulfide bond; Electron transport; FAD; Flavoprotein; Membrane; NADP;
KW Oxidoreductase; Phosphoprotein; Photosynthesis; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 50..360
FT /note="Ferredoxin--NADP reductase, leaf isozyme 1,
FT chloroplastic"
FT /id="PRO_0000322572"
FT DOMAIN 81..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 139..142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 160..162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 177..179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00455"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 250..251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 280..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 319..320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT DISULFID 178..183
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="A -> S (in Ref. 5; BAE98556)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> G (in Ref. 1; CAB52472)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..278
FT /note="DFA -> GFS (in Ref. 1; CAB52472)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="Y -> F (in Ref. 1; CAB52472)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="Y -> F (in Ref. 1; CAB52472)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="Y -> F (in Ref. 1; CAB52472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40326 MW; F50B5C79476283ED CRC64;
MAAAISAAVS LPSSKSSSLL TKISSVSPQR IFLKKSTVCY RRVVSVKAQV TTDTTEAPPV
KVVKESKKQE EGIVVNKFKP KNPYTGRCLL NTKITGDDAP GETWHIVFTT EGEVPYREGQ
SIGVIPEGID KNGKPHKLRL YSIASSAIGD FGDSKTVSLC VKRLVYTNDG GEIVKGVCSN
FLCDLKPGDE AKITGPVGKE MLMPKDPNAT IIMLGTGTGI APFRSFLWKM FFEEHEDYKF
NGLAWLFLGV PTSSSLLYKE EFEKMKEKNP DNFRLDFAVS REQTNEKGEK MYIQTRMAEY
AEELWELLKK DNTFVYMCGL KGMEKGIDDI MVSLAAKDGI DWLEYKKQLK RSEQWNVEVY
