[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1104/pp.106.4.1715; PubMed=7846183 [NCBI, ExPASy, EBI, Israel, Japan] Kitayama M., Kitayama K., Togasaki R.K.; "A cDNA clone encoding a ferredoxin-NADP+ reductase from Chlamydomonas reinhardtii."; Plant Physiol. 106:1715-1716(1994).
[2]	PROTEIN SEQUENCE OF 36-265, AND METHYLATION AT LYS-118; LYS-124 AND LYS-170. Decottignies P., Flesch V., Jacquot J.-P., Schmitter J.-M., le Marechal P.; "Specific post-translational methylation of three lysine residues in Chlamydomonas reinhardtii ferredoxin-NADP reductase."; (In) Proceedings of XIth international conference on methods in protein structure analysis, pp.45-45, Annecy (1996).

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

U10545; AAA79131.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T08035; T08035.

3D structure databases

HSSP

Q41736; 1JB9. [HSSP ENTRY / PDB]

ModBase

P53991.

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).

Proteomics databases

PRIDE

P53991; -.

Other

ProtoNet

P53991.

UniRef

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

Keywords

Chloroplast; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Membrane; Methylation; NADP; Oxidoreductase; Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 35`	`35`	`Chloroplast.`
`CHAIN`	`36 354`	`319`	`Ferredoxin--NADP reductase, chloroplastic.`	`PRO_0000019407`
`DOMAIN`	`69 198`	`130`	`FAD-binding FR-type.`
`NP_BIND`	`130 133`	`4`	`FAD (By similarity).`
`NP_BIND`	`151 153`	`3`	`FAD (By similarity).`
`NP_BIND`	`172 174`	`3`	`FAD (By similarity).`
`NP_BIND`	`245 246`	`2`	`NADP (By similarity).`
`NP_BIND`	`275 276`	`2`	`NADP (By similarity).`
`NP_BIND`	`313 314`	`2`	`NADP (By similarity).`
`BINDING`	`133 133`		`NADP (By similarity).`
`BINDING`	`153 153`		`NADP (By similarity).`
`BINDING`	`157 157`		`FAD (By similarity).`
`BINDING`	`213 213`		`FAD (By similarity).`
`BINDING`	`213 213`		`NADP; via amide nitrogen (By similarity).`
`BINDING`	`285 285`		`NADP (By similarity).`
`BINDING`	`352 352`		`NADP (By similarity).`
`MOD_RES`	`118 118`		`N6,N6,N6-trimethyllysine.`
`MOD_RES`	`124 124`		`N6,N6,N6-trimethyllysine.`
`MOD_RES`	`170 170`		`N6,N6-dimethyllysine.`

Sequence information

Length: 354 AA [This is the length of the unprocessed precursor]

Molecular weight: 39277 Da [This is the MW of the unprocessed precursor]

CRC64: 4927FBA0CF668FBD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASLRKPSNH ADRACSRRLR VATRVAGRRM CRPVAATKAS TAVTTDMSKR TVPTKLEEGE 

        70         80         90        100        110        120 
MPLNTYSNKA PFKAKVRSVE KITGPKATGE TCHIIIETEG KIPFWEGQSY GVIPPGTKIN 

       130        140        150        160        170        180 
SKGKEVPTAR LYSIASSRYG DDGDGQTASL CVRRAVYVDP ETGKEDPAKK GLCSNFLCDA 

       190        200        210        220        230        240 
TPGTEISMTG PTGKVLLLPA DANAPLICVA TGTGIAPFRS FWRRCFIENV PSYKFTGLFW 

       250        260        270        280        290        300 
LFMGVGNSDA KLYDEELQAI AKAYPGQFRL DYALSREQNN RKGGKMYIQD KVEEYADEIF 

       310        320        330        340        350 
DLLDNGAHMY FCGLKGMMPG IQDMLERVAK EKGLNYEEWV EGLKHKNQWH VEVY

P53991 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