[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Kinmaze; TISSUE=Leaf; DOI=10.1104/pp.104.4.1473; PubMed=8016278 [NCBI, ExPASy, EBI, Israel, Japan] Aoki H., Doyama N., Ida S.; "Sequence of a cDNA encoding rice (Oryza sativa L.) leaf ferredoxin-NADP+ reductase."; Plant Physiol. 104:1473-1474(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; The international rice genome sequencing project (IRGSP) consortium; "Oryza sativa nipponbare chromosome 6 genomic DNA sequence."; Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: May play 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.
PATHWAY: Energy metabolism; photosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side (Probable). Note=In the vicinity of the photosystem I in the non-stacked and fringe portion of the 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

D17790; BAA04616.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000616; BAA85425.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001129; BAA90642.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T04349; T04349.

NP_001056570.1; -.

3D structure databases

HSSP

Q9SLP6; 1GAQ. [HSSP ENTRY / PDB]

SMR

P41344; 58-362.

ModBase

P41344.

Organism-specific databases

Gramene

P41344; -.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0042651;	Cellular component: thylakoid membrane (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004324;	Molecular function: ferredoxin-NADP+ reductase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
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

IPR001834; Cyt_B5_reductase.
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

PR00406; CYTB5RDTASE.
PR00371; FPNCR.

PROSITE

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

ProtoNet

P41344.

Genome annotation databases

GeneID

4339874; -.

KEGG

osa:4339874; -.

Other

UniRef

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

Keywords

Chloroplast; 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 62`	`62`	`Chloroplast (Potential).`
`CHAIN`	`63 362`	`300`	`Ferredoxin--NADP reductase, leaf isozyme, chloroplastic.`	`PRO_0000019409`
`DOMAIN`	`83 205`	`123`	`FAD-binding FR-type.`
`NP_BIND`	`214 232`	`19`	`NADP (By similarity).`
`DISULFID`	`180 185`		`By similarity.`

Sequence information

Length: 362 AA [This is the length of the unprocessed precursor]

Molecular weight: 40008 Da [This is the MW of the unprocessed precursor]

CRC64: 1B6034A8A76E4F29 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVTAAAVS TSAAAAVTKA SPSPAHCFLP CPPRTRAAHQ RGLLLRAQVS TTDAAAVAAA 

        70         80         90        100        110        120 
PAKKEKISKK HDEGVVTNKY RPKEPYVGKC LLNTKITADD APGETWHMVF STEGEIPYRE 

       130        140        150        160        170        180 
GQSIGVIADG VDKNGKPHKL RLYSIASSAL GDFGDSKTVS LCVKRLVYTN DQGEIVKGVC 

       190        200        210        220        230        240 
SNFLCDLKPG SDVKITGPVG KEMLMPKDPN ANIIMLATGT GIAPFRSFLW KMFFEKYDDY 

       250        260        270        280        290        300 
KFNGLAWLFL GVPTSSSLLY KEEFDKMKAK APENFRVDYA VSREQTNAQG EKMYIQTRMA 

       310        320        330        340        350        360 
EYKEELWELL KKDHTYVYMC GLKGMEKGID DIMVSLAAKD GIDWADYKKQ LKKGEQWNVE 


VY

P41344 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