[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Bright Yellow 2; Kumada H.O., Aoki H., Doyama N., Ida S.; "Nucleotide sequence of a ferredoxin-NADP+ oxidoreductase cDNA from cultured tobacco cells."; (er) Plant Gene Register PGR98-038.

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. Is involved in nitrate assimilation.
CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP⁺ + H⁺ = 2 oxidized ferredoxin + NADPH.
COFACTOR: FAD.
PATHWAY: Energy metabolism; photosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
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

AB004307; BAA20365.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T02215; T02215.

3D structure databases

HSSP

Q41736; 1JB9. [HSSP ENTRY / PDB]

SMR

O04397; 66-375.

ModBase

O04397.

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).

Other

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

Keywords

Chloroplast; Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase; Photosynthesis; Plastid; Transit peptide; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 60`	`60`	`Chloroplast (Potential).`
`CHAIN`	`61 375`	`315`	`Ferredoxin--NADP reductase, root-type isozyme, chloroplastic.`	`PRO_0000019416`
`DOMAIN`	`91 219`	`129`	`FAD-binding FR-type.`
`NP_BIND`	`229 247`	`19`	`NADP (By similarity).`
`DISULFID`	`194 199`		`By similarity.`

Sequence information

Length: 375 AA [This is the length of the unprocessed precursor]

Molecular weight: 41958 Da [This is the MW of the unprocessed precursor]

CRC64: AB5ED3988F746B92 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAHSALSQVS VAVPLQTDSS FRRSTFKATS ITFSDRSSWI SMPPIDLKAA PSRNQHIVCM 

        70         80         90        100        110        120 
SVQQASKAKV SVSPLSLEDA KEPPLNIYKP KEPYTATIVS VERLVGPKAP GETCHIVIDH 

       130        140        150        160        170        180 
DGNLPYWEGQ SYGVIPPGEN PKKPGNPHNV RLYLIASTRY GDSFDGKTAS LCVRRAVYYD 

       190        200        210        220        230        240 
PETGKEDPSK NGVCSNFLCD SKPGDKVKIT GPSGKIMLLP EEIPNATHIM IGTGTGVAPF 

       250        260        270        280        290        300 
RGYLRRMFME SVPTKFNGLA WLFLGVANTD SLLYDDEFTK YLNDYPGNFR YDRALSREQK 

       310        320        330        340        350        360 
NNKGGKMYVQ DKIEEYSDEI FKLLDEGAHI YFCGLKGMMP GIQDTLKRVA ERRGESWEQK 

       370 
LSQLKKNKQW HVEVY

O04397 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