FNRR1_ARATH
ID FNRR1_ARATH Reviewed; 378 AA.
AC Q9M0V6; Q8L7D9; Q8LBD8; Q8VY95;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ferredoxin--NADP reductase, root isozyme 1, chloroplastic;
DE EC=1.18.1.2;
DE AltName: Full=Root FNR 1;
DE Short=AtRFNR1;
DE Flags: Precursor;
GN Name=RFNR1; Synonyms=PETH3; OrderedLocusNames=At4g05390; ORFNames=C6L9.70;
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=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 [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).
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 FUNCTION, INDUCTION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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).
CC -!- FUNCTION: Maintains the supply of reduced ferredoxin under non-
CC photosynthetic conditions. {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;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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=Q9M0V6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoots and roots. Less abundant in
CC roots than RFNR2. {ECO:0000269|Ref.5}.
CC -!- INDUCTION: Up-regulated by nitrate in roots while down-regulated in
CC shoots. {ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81081.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL161503; CAB81081.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82512.1; -; Genomic_DNA.
DR EMBL; AY072339; AAL61946.1; -; mRNA.
DR EMBL; AY114609; AAM47928.1; -; mRNA.
DR EMBL; AY136312; AAM96978.1; -; mRNA.
DR EMBL; AY087271; AAM64825.1; -; mRNA.
DR PIR; G85067; G85067.
DR RefSeq; NP_567293.1; NM_116778.4. [Q9M0V6-1]
DR AlphaFoldDB; Q9M0V6; -.
DR SMR; Q9M0V6; -.
DR BioGRID; 11198; 3.
DR STRING; 3702.AT4G05390.1; -.
DR MetOSite; Q9M0V6; -.
DR PaxDb; Q9M0V6; -.
DR PRIDE; Q9M0V6; -.
DR ProteomicsDB; 230631; -. [Q9M0V6-1]
DR EnsemblPlants; AT4G05390.1; AT4G05390.1; AT4G05390. [Q9M0V6-1]
DR GeneID; 825887; -.
DR Gramene; AT4G05390.1; AT4G05390.1; AT4G05390. [Q9M0V6-1]
DR KEGG; ath:AT4G05390; -.
DR Araport; AT4G05390; -.
DR TAIR; locus:2115964; AT4G05390.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; Q9M0V6; -.
DR OrthoDB; 817123at2759; -.
DR PhylomeDB; Q9M0V6; -.
DR BioCyc; ARA:AT4G05390-MON; -.
DR PRO; PR:Q9M0V6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0V6; baseline and differential.
DR Genevisible; Q9M0V6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Coiled coil; Disulfide bond;
KW Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Phosphoprotein; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..378
FT /note="Ferredoxin--NADP reductase, root isozyme 1,
FT chloroplastic"
FT /id="PRO_0000322574"
FT DOMAIN 93..221
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT COILED 349..373
FT /evidence="ECO:0000255"
FT BINDING 231..249
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT DISULFID 196..201
FT /evidence="ECO:0000250"
FT CONFLICT 132
FT /note="Q -> K (in Ref. 4; AAM64825)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="D -> N (in Ref. 3; AAM96978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42396 MW; 187388432B71968D CRC64;
MALSTTPSQM SVALPTRIDG SSRSMIKVQS ISFTDKSWGP PLLRLDSKSR SLGVKKRSTI
CMSLQQSSKS KVLVTPLELE DPKETPLNLF RPKEPYTATI VSVERIVGPQ APGETCHIVI
DHDGNVPYWE GQSYGVIPPG ENPKKPGAPH NVRLYSIAST RYGDSFDGKT ASLCVRRAIY
YDPETGKEDP SKAGVCSNFL CNAKPGDKVK ITGPSGKVML LPEDDPKATH IMIATGTGVA
PYRGYLRRMF MENVPNFKFD GLAWLFLGVA NSDSLLYDEE FAGYRKDYPE NFRYDKALSR
EEKNKKGGKM YVQDKIEEYS DEIFKLLDNG AHIYFCGLKG MMPGIQDTLK RVAEERGESW
EQKLTQLRKN KQWHVEVY
