FNRL2_ARATH
ID FNRL2_ARATH Reviewed; 369 AA.
AC Q8W493; A8MRF7; A8MRG5; Q9LNS9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic;
DE EC=1.18.1.2 {ECO:0000269|Ref.5};
DE AltName: Full=Leaf FNR 2 {ECO:0000303|Ref.5};
DE Short=AtLFNR2 {ECO:0000303|Ref.5};
DE Short=FNR-2 {ECO:0000303|Ref.5};
DE Flags: Precursor;
GN Name=LFNR2 {ECO:0000303|Ref.5}; Synonyms=PETH2;
GN OrderedLocusNames=At1g20020 {ECO:0000312|Araport:AT1G20020};
GN ORFNames=T20H2.20 {ECO:0000312|EMBL:AAF79911.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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 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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, PROTEIN SEQUENCE OF 58-67, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
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 [7]
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 [8]
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 [9]
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 [10]
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.5}.
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.5};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 uM for ferredoxin-1 {ECO:0000269|Ref.5};
CC KM=3.5 uM for ferredoxin-2 {ECO:0000269|Ref.5};
CC KM=5.4 uM for ferredoxin-3 {ECO:0000269|Ref.5};
CC -!- PATHWAY: Energy metabolism; photosynthesis. {ECO:0000269|Ref.5}.
CC -!- SUBUNIT: Heterodimer with LFNR1. 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 LFNR1 and LFNR2; LIR1
CC increases the affinity of LFNR1 and LFNR2 for TIC62 and subsequent
CC thylakoid relocalization (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZFJ3, 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.5}.
CC Plastid, chloroplast thylakoid membrane {ECO:0000269|Ref.5}; Peripheral
CC membrane protein {ECO:0000269|Ref.5}; Stromal side {ECO:0000269|Ref.5}.
CC Note=More abundant in the soluble fraction. The presence of LFNR1 is
CC required for association with the thylakoid membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8W493-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W493-2; Sequence=VSP_031937;
CC Name=3;
CC IsoId=Q8W493-3; Sequence=VSP_031936;
CC -!- TISSUE SPECIFICITY: Expressed in shoots. Restricted to green tissues,
CC being more abundant in stems. {ECO:0000269|Ref.5}.
CC -!- INDUCTION: By nitrate. {ECO:0000269|PubMed:10948265}.
CC -!- PTM: May form interchain disulfide bonds with LIR1.
CC {ECO:0000250|UniProtKB:Q9FKW6}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79911.1; Type=Erroneous gene model prediction; Evidence={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; AC022472; AAF79911.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29923.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29925.1; -; Genomic_DNA.
DR EMBL; AY062739; AAL32817.1; -; mRNA.
DR EMBL; AY114663; AAM47982.1; -; mRNA.
DR PIR; F86333; F86333.
DR RefSeq; NP_001077566.1; NM_001084097.1. [Q8W493-3]
DR RefSeq; NP_173431.1; NM_101857.6. [Q8W493-1]
DR AlphaFoldDB; Q8W493; -.
DR SMR; Q8W493; -.
DR BioGRID; 23830; 6.
DR IntAct; Q8W493; 2.
DR STRING; 3702.AT1G20020.1; -.
DR iPTMnet; Q8W493; -.
DR MetOSite; Q8W493; -.
DR World-2DPAGE; 0003:Q8W493; -.
DR PaxDb; Q8W493; -.
DR PRIDE; Q8W493; -.
DR ProteomicsDB; 230591; -. [Q8W493-1]
DR EnsemblPlants; AT1G20020.1; AT1G20020.1; AT1G20020. [Q8W493-1]
DR EnsemblPlants; AT1G20020.3; AT1G20020.3; AT1G20020. [Q8W493-3]
DR GeneID; 838591; -.
DR Gramene; AT1G20020.1; AT1G20020.1; AT1G20020. [Q8W493-1]
DR Gramene; AT1G20020.3; AT1G20020.3; AT1G20020. [Q8W493-3]
DR KEGG; ath:AT1G20020; -.
DR Araport; AT1G20020; -.
DR TAIR; locus:2198651; AT1G20020.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_053066_0_0_1; -.
DR InParanoid; Q8W493; -.
DR OMA; CVKRHRY; -.
DR OrthoDB; 817123at2759; -.
DR PhylomeDB; Q8W493; -.
DR BioCyc; ARA:AT1G20020-MON; -.
DR BRENDA; 1.18.1.2; 399.
DR UniPathway; UPA00091; -.
DR PRO; PR:Q8W493; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W493; baseline and differential.
DR Genevisible; Q8W493; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; 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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA: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:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniPathway.
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..57
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 58..369
FT /note="Ferredoxin--NADP reductase, leaf isozyme 2,
FT chloroplastic"
FT /id="PRO_0000322573"
FT DOMAIN 90..212
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 148..151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 169..171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 186..188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00455"
FT BINDING 227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 259..260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 289..290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 299
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 328..329
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 367
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT DISULFID 187..192
FT /evidence="ECO:0000250"
FT VAR_SEQ 122
FT /note="E -> K (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_031936"
FT VAR_SEQ 147..165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031937"
SQ SEQUENCE 369 AA; 41168 MW; DA49E26B60F9CF73 CRC64;
MATTMNAAVS LTSSNSSSFP ATSCAIAPER IRFTKGAFYY KSNNVVTGKR VFSIKAQITT
ETDTPTPAKK VEKVSKKNEE GVIVNRYRPK EPYTGKCLLN TKITADDAPG ETWHMVFSHQ
GEIPYREGQS VGVIADGIDK NGKPHKVRLY SIASSALGDL GNSETVSLCV KRLVYTNDQG
ETVKGVCSNF LCDLAPGSDV KLTGPVGKEM LMPKDPNATV IMLATGTGIA PFRSFLWKMF
FEKHDDYKFN GLAWLFLGVP TTSSLLYQEE FDKMKAKAPE NFRVDYAISR EQANDKGEKM
YIQTRMAQYA AELWELLKKD NTFVYMCGLK GMEKGIDDIM VSLAANDGID WFDYKKQLKK
AEQWNVEVY
