[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; Legen J., Misera S., Herrmann R.G., Altschmied L.; "Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding organellar polypeptides."; Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/5.2.131; PubMed=9679202 [NCBI, ExPASy, EBI, Israel, Japan] Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."; DNA Res. 5:131-145(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan] Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; "Empirical analysis of transcriptional activity in the Arabidopsis genome."; Science 302:842-846(2003).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.; "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]	INDUCTION BY NITRATE. DOI=10.1105/tpc.12.8.1491; PubMed=10948265 [NCBI, ExPASy, EBI, Israel, Japan] Wang R., Guegler K., LaBrie S.T., Crawford N.M.; "Genomic analysis of a nutrient response in Arabidopsis reveals diverse expression patterns and novel metabolic and potential regulatory genes induced by nitrate."; Plant Cell 12:1491-1509(2000).
[6]	IDENTIFICATION. DOI=10.1105/tpc.017814; PubMed=14729914 [NCBI, ExPASy, EBI, Israel, Japan] Friso G., Giacomelli L., Ytterberg A.J., Peltier J.-B., Rudella A., Sun Q., van Wijk K.J.; "In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database."; Plant Cell 16:478-499(2004).
[7]	FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY, PROTEIN SEQUENCE OF 49-59, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, AND NOMENCLATURE. STRAIN=cv. Columbia; Hanke G.T., Okutani S., Satomi Y., Takao T., Suzuki A., Hase T.; "Multiple iso-proteins of FNR in Arabidopsis: evidence for different contributions to chloroplast function and nitrogen assimilation."; Plant Cell Environ. 28:1146-1157(2005).
[8]	FUNCTION, MASS SPECTROMETRY, AND SUBUNIT. DOI=10.1111/j.1365-313X.2006.03014.x; PubMed=17335513 [NCBI, ExPASy, EBI, Israel, Japan] Lintala M., Allahverdiyeva Y., Kidron H., Piippo M., Battchikova N., Suorsa M., Rintamaeki E., Salminen T.A., Aro E.-M., Mulo P.; "Structural and functional characterization of ferredoxin-NADP+-oxidoreductase using knock-out mutants of Arabidopsis."; Plant J. 49:1041-1052(2007).
[9]	INTERACTION WITH PGRL1A AND PGRL1B. STRAIN=cv. Columbia; DOI=10.1016/j.cell.2007.12.028; PubMed=18243102 [NCBI, ExPASy, EBI, Israel, Japan] DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D., Finazzi G., Joliot P., Barbato R., Leister D.; "A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis."; Cell 132:273-285(2008).

Comments

FUNCTION: Plays a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP⁺ + H⁺ = 2 oxidized ferredoxin + NADPH.
COFACTOR: FAD.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=3.5 µM for ferredoxin-1;
K_M=2.5 µM for ferredoxin-2;
K_M=4.6 µM for ferredoxin-3;
PATHWAY: Energy metabolism; photosynthesis .
SUBUNIT: Heterodimer with LFNR2. Interacts with PGRL1A and PGRL1B.
SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. Note=More abundant in the membrane fraction.
ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. A number of isoforms are produced. According to EST sequences.

Name 1

Isoform ID Q9FKW6-1

This is the isoform sequence displayed in this entry.
TISSUE SPECIFICITY: Expressed in shoots. Restricted to green tissues, being more abundant in siliques.
INDUCTION: By nitrate.
MISCELLANEOUS: Loss-of-function mutant deltaFNR1 (T-DNA insertion) has a reduced capacity for carbon fixation and prevent the association of LFNR2 with the thylakoid membrane.
SIMILARITY: Belongs to the ferredoxin--NADP reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ243705; CAB52472.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB011474; BAB10424.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY072112; AAL59934.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY096665; AAM20299.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK226411; BAE98556.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_201420.1; -.

UniGene

At.47570

3D structure databases

HSSP

P10933; 1QGA. [HSSP ENTRY / PDB]

SMR

Q9FKW6; 54-359.

ModBase

Q9FKW6.

Protein-protein interaction databases

IntAct

Q9FKW6; -.

Organism-specific databases

TAIR

At5g66190; -.

Gene expression databases

ArrayExpress

Q9FKW6; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0015979;	Biological process: photosynthesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001709; FPN_cyt_redctse.
IPR012146; Frd-NADP+_RD.
IPR015701; FRD_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

PANTHER

PTHR19384:SF1; FRD_Red; 1.

Pfam

PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000361; Frd-NADP+_RD; 1.

PRINTS

PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

836751; -.

GenomeReviews

BA000015_GR; AT5G66190.

NMPDR

fig|3702.1.peg.28717; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Chloroplast; Complete proteome; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; NADP; Oxidoreductase; Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 49`	`49`	`Chloroplast.`
`CHAIN`	`50 360`	`311`	`Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic.`	`PRO_0000322572`
`DOMAIN`	`81 203`	`123`	`FAD-binding FR-type.`
`NP_BIND`	`212 230`	`19`	`NADP (By similarity).`
`DISULFID`	`178 183`		`By similarity.`
`CONFLICT`	`2 2`		`A -> S (in Ref. 4; BAE98556).`
`CONFLICT`	`113 113`		`E -> G (in Ref. 1; CAB52472).`
`CONFLICT`	`276 278`		`DFA -> GFS (in Ref. 1; CAB52472).`
`CONFLICT`	`292 292`		`Y -> F (in Ref. 1; CAB52472).`
`CONFLICT`	`345 345`		`Y -> F (in Ref. 1; CAB52472).`
`CONFLICT`	`360 360`		`Y -> F (in Ref. 1; CAB52472).`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 40326 Da [This is the MW of the unprocessed precursor]

CRC64: F50B5C79476283ED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAISAAVS LPSSKSSSLL TKISSVSPQR IFLKKSTVCY RRVVSVKAQV TTDTTEAPPV 

        70         80         90        100        110        120 
KVVKESKKQE EGIVVNKFKP KNPYTGRCLL NTKITGDDAP GETWHIVFTT EGEVPYREGQ 

       130        140        150        160        170        180 
SIGVIPEGID KNGKPHKLRL YSIASSAIGD FGDSKTVSLC VKRLVYTNDG GEIVKGVCSN 

       190        200        210        220        230        240 
FLCDLKPGDE AKITGPVGKE MLMPKDPNAT IIMLGTGTGI APFRSFLWKM FFEEHEDYKF 

       250        260        270        280        290        300 
NGLAWLFLGV PTSSSLLYKE EFEKMKEKNP DNFRLDFAVS REQTNEKGEK MYIQTRMAEY 

       310        320        330        340        350        360 
AEELWELLKK DNTFVYMCGL KGMEKGIDDI MVSLAAKDGI DWLEYKKQLK RSEQWNVEVY

Q9FKW6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools