Reviewed, UniProtKB/Swiss-Prot Q9FKW6 (FNRL1_ARATH)

Names and origin

Protein names

Recommended name:
    Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
    EC=1.18.1.2
Alternative name(s):
    Leaf FNR 1
      Short name=AtLFNR1
      Short name=FNR-1

Gene names

Name:	LFNR1
Synonyms:	PETH1
Ordered Locus Names:	At5g66190
ORF Names:	K2A18.27

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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. Ref.7 Ref.8
Catalytic activity	2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.
Cofactor	FAD.
Pathway	Energy metabolism; photosynthesis.
Subunit structure	Heterodimer with LFNR2. Interacts with PGRL1A and PGRL1B. Ref.8 Ref.9
Subcellular location	Plastid › chloroplast stroma. Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. Note: More abundant in the membrane fraction. Ref.7
Tissue specificity	Expressed in shoots. Restricted to green tissues, being more abundant in siliques. Ref.7
Induction	By nitrate. Ref.5
Disruption phenotype	Plants have a reduced capacity for carbon fixation and prevent the association of LFNR2 with the thylakoid membrane. Ref.8
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 1 family. Contains 1 FAD-binding FR-type domain.
Biophysicochemical properties	Kinetic parameters: KM=3.5 µM for ferredoxin-1 KM=2.5 µM for ferredoxin-2 KM=4.6 µM for ferredoxin-3

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Chloroplast Membrane Plastid Thylakoid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from expression pattern. Source: TAIR electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR chloroplast thylakoid membrane Ref.6 Inferred from direct assay. Source: TAIR thylakoid lumen Inferred from direct assay. Source: TAIR
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Ref.8 Inferred from direct assay. Source: TAIR electron transporter, transferring electrons within the noncyclic electron transport pathway of photosynthesis activity Ref.8 Inferred from direct assay. Source: TAIR ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: EC poly(U) binding Inferred from direct assay. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FKW6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 49	49	Chloroplast
	Chain	50 – 360	311	Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic		PRO_0000322572
Regions
	Domain	81 – 203	123	FAD-binding FR-type
	Nucleotide binding	212 – 230	19	NADP By similarity
Amino acid modifications
	Disulfide bond	178 ↔ 183		By similarity
Experimental info
	Sequence conflict	2	1	A → S in BAE98556. Ref.4
	Sequence conflict	113	1	E → G in CAB52472. Ref.1
	Sequence conflict	276 – 278	3	DFA → GFS in CAB52472. Ref.1
	Sequence conflict	292	1	Y → F in CAB52472. Ref.1
	Sequence conflict	345	1	Y → F in CAB52472. Ref.1
	Sequence conflict	360	1	Y → F in CAB52472. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F50B5C79476283ED	FASTA	360	40,326
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding organellar polypeptides." Legen J., Misera S., Herrmann R.G., Altschmied L. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"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." Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:131-145(1998) [PubMed: 9679202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." 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. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Genomic analysis of a nutrient response in Arabidopsis reveals diverse expression patterns and novel metabolic and potential regulatory genes induced by nitrate." Wang R., Guegler K., LaBrie S.T., Crawford N.M. Plant Cell 12:1491-1509(2000) [PubMed: 10948265] [Abstract] Cited for: INDUCTION BY NITRATE.
[6]	"In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database." Friso G., Giacomelli L., Ytterberg A.J., Peltier J.-B., Rudella A., Sun Q., van Wijk K.J. Plant Cell 16:478-499(2004) [PubMed: 14729914] [Abstract] Cited for: IDENTIFICATION.
[7]	"Multiple iso-proteins of FNR in Arabidopsis: evidence for different contributions to chloroplast function and nitrogen assimilation." Hanke G.T., Okutani S., Satomi Y., Takao T., Suzuki A., Hase T. Plant Cell Environ. 28:1146-1157(2005) Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY, PROTEIN SEQUENCE OF 49-59, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE. Strain: cv. Columbia.
[8]	"Structural and functional characterization of ferredoxin-NADP+-oxidoreductase using knock-out mutants of Arabidopsis." Lintala M., Allahverdiyeva Y., Kidron H., Piippo M., Battchikova N., Suorsa M., Rintamaeki E., Salminen T.A., Aro E.-M., Mulo P. Plant J. 49:1041-1052(2007) [PubMed: 17335513] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY, SUBUNIT, DISRUPTION PHENOTYPE.
[9]	"A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis." DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D., Finazzi G., Joliot P., Barbato R., Leister D. Cell 132:273-285(2008) [PubMed: 18243102] [Abstract] Cited for: INTERACTION WITH PGRL1A AND PGRL1B. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ243705 mRNA. Translation: CAB52472.1. AB011474 Genomic DNA. Translation: BAB10424.1. AY072112 mRNA. Translation: AAL59934.1. AY096665 mRNA. Translation: AAM20299.1. AK226411 mRNA. Translation: BAE98556.1.
IPI	IPI00541856.
RefSeq	NP_201420.1.
UniGene	At.47570 At.49233
3D structure databases
HSSP	HSSP built from PDB template 1QGA based on UniProtKB P10933.
SMR	Q9FKW6. Positions 54-359.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FKW6. 1 interaction.
Proteomic databases
PRIDE	Q9FKW6.
Genome annotation databases
GeneID	836751.
GenomeReviews	Gene locus AT5G66190 in contig BA000015_GR.
NMPDR	fig|3702.1.peg.28717.
Organism-specific databases
TAIR	At5g66190.
Phylogenomic databases
OMA	Q9FKW6. NEDANAN.
Enzyme and pathway databases
BRENDA	1.18.1.2. 302.
Gene expression databases
ArrayExpress	Q9FKW6.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012146. Frd-NADP+_RD. IPR015701. FRD_Red. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
PANTHER	PTHR19384:SF1. FRD_Red. 1 hit.
Pfam	PF00175. NAD_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTS	PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FNRL1_ARATH

Accession

Primary (citable) accession number: Q9FKW6
Secondary accession number(s): Q0WWE2, Q9SUJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)