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

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Cross-references

Sequence databases

EMBL

U14956; AAA21758.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P10933; 1QG0. [HSSP ENTRY / PDB]

SMR

P41346; 55-362.

ModBase

P41346.

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

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).

ProtoNet

P41346.

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 52`	`52`	`Chloroplast (Potential).`
`CHAIN`	`53 363`	`311`	`Ferredoxin--NADP reductase, chloroplastic.`	`PRO_0000019410`
`DOMAIN`	`84 206`	`123`	`FAD-binding FR-type.`
`NP_BIND`	`215 233`	`19`	`NADP (By similarity).`
`DISULFID`	`181 186`		`By similarity.`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 40579 Da [This is the MW of the unprocessed precursor]

CRC64: CB0C8CC6D3203063 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNS VSISGRVGTI RAQITTEAEA 

        70         80         90        100        110        120 
PVTKVVKHSK KQDEGIVVNK FKPKEPYVGR CLLNTKITGD DAPGETWHMV FTTEGEVPYR 

       130        140        150        160        170        180 
EGQSIGIVPD GIDKNGKPHK LRLYSIASSA IGDFGDSKTV SLCVKRLVYT NDAGEVVKGV 

       190        200        210        220        230        240 
CSNFLCDLKP GSEVKITGPV GKEMLMPKDP NATVIMLGTG TGIAPFRSFL WKMFFEKHED 

       250        260        270        280        290        300 
YKFNGLAWLF LGVPTSSSLL YKEEFEKMKE KAPENFRLDF AVSREQVNDK GEKMYIQTRM 

       310        320        330        340        350        360 
AQYAEELWEL LKKDNTFVYM CGLKGMEKGI DDIMVSIRPK DGIDWIEYKR TLKKAEQWNV 


EVY

P41346 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