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P00455 (FENR_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferredoxin--NADP reductase, chloroplastic

Short name=FNR
EC=1.18.1.2
Gene names
Name:PETH
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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

Plastidchloroplast stroma. Plastidchloroplast 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.

Miscellaneous

FNR is probably attached to the membrane by a specific binding protein.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Contains 1 FAD-binding FR-type domain.

Biophysicochemical properties

Kinetic parameters:

KM=35 µM for NADPH Ref.5

Ontologies

Keywords
   Biological processElectron transport
Photosynthesis
Transport
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   DomainTransit peptide
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processphotosynthesis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast stroma

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 10451365PubMed 8174709. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PETFP002213EBI-865079,EBI-864933

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5555Chloroplast Ref.3
Chain56 – 369314Ferredoxin--NADP reductase, chloroplastic
PRO_0000019412

Regions

Domain90 – 212123FAD-binding FR-type
Nucleotide binding148 – 1514FAD
Nucleotide binding169 – 1713FAD
Nucleotide binding186 – 1883FAD
Nucleotide binding259 – 2602NADP
Nucleotide binding289 – 2902NADP
Nucleotide binding299 – 3013NADP
Nucleotide binding328 – 3292NADP By similarity

Sites

Binding site1511NADP By similarity
Binding site1711NADP
Binding site1751FAD
Binding site2271FAD
Binding site2271NADP; via amide nitrogen By similarity
Binding site3671NADP By similarity

Natural variations

Natural variant3241F → V.

Experimental info

Mutagenesis3671E → A: Slightly reduced activity. Ref.6
Mutagenesis3671E → D or Q: Reduced activity. Ref.6
Mutagenesis3671E → L: Reduces activity by 99%. Ref.6

Secondary structure

........................................................ 369
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00455 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 1D0432BA47438A28

FASTA36941,188
        10         20         30         40         50         60 
MTTAVTAAVS FPSTKTTSLS ARSSSVISPD KISYKKVPLY YRNVSATGKM GPIRAQIASD 

        70         80         90        100        110        120 
VEAPPPAPAK VEKHSKKMEE GITVNKFKPK TPYVGRCLLN TKITGDDAPG ETWHMVFSHE 

       130        140        150        160        170        180 
GEIPYREGQS VGVIPDGEDK NGKPHKLRLY SIASSALGDF GDAKSVSLCV KRLIYTNDAG 

       190        200        210        220        230        240 
ETIKGVCSNF LCDLKPGAEV KLTGPVGKEM LMPKDPNATI IMLGTGTGIA PFRSFLWKMF 

       250        260        270        280        290        300 
FEKHDDYKFN GLAWLFLGVP TSSSLLYKEE FEKMKEKAPD NFRLDFAVSR EQTNEKGEKM 

       310        320        330        340        350        360 
YIQTRMAQYA VELWEMLKKD NTYFYMCGLK GMEKGIDDIM VSLAAAEGID WIEYKRQLKK 


AEQWNVEVY 

« Hide

References

[1]"Analysis of cDNA clones encoding the entire precursor-polypeptide for ferredoxin:NADP+ oxidoreductase from spinach."
Jansen T., Reilaender H., Steppuhn J., Herrmann R.G.
Curr. Genet. 13:517-522(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and sequencing of the cDNA for precursor ferredoxin-NADP+: oxidoreductase from spinach."
Alter J.M., Patrie W.J.
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase."
Karplus P.A., Walsh K.A., Herriott J.R.
Biochemistry 23:6576-6583(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 56-369.
[4]"Characterization of the promoter from the single-copy gene encoding ferredoxin-NADP(+)-oxidoreductase from spinach."
Oelmueller R., Bolle C., Tyagi A.K., Niekrawietz N., Breit S.
Mol. Gen. Genet. 237:261-272(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
[5]"Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family."
Karplus P.A., Daniels M.J., Herriott J.R.
Science 251:60-66(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND 2-PHOSPHO-AMP, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase."
Aliverti A., Deng Z., Ravasi D., Piubelli L., Karplus P.A., Zanetti G.
J. Biol. Chem. 273:34008-34015(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-369 OF MUTANTS ALA/GLN/LEU-367 IN COMPLEX WITH FAD, MUTAGENESIS OF GLU-367.
Tissue: Leaf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07981 mRNA. Translation: CAA30791.1.
M86349 mRNA. Translation: AAA34029.1.
X64351 Genomic DNA. Translation: CAA45703.1.
PIRRDSPXX. S00438.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX0X-ray1.90A56-369[»]
1BX1X-ray1.90A56-369[»]
1FNBX-ray1.70A56-369[»]
1FNCX-ray2.00A56-369[»]
1FNDX-ray1.70A56-369[»]
1FRNX-ray2.00A56-369[»]
1FRQX-ray1.95A56-369[»]
ProteinModelPortalP00455.
SMRP00455. Positions 74-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00455. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00455.
UniPathwayUPA00091.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00455.

Entry information

Entry nameFENR_SPIOL
AccessionPrimary (citable) accession number: P00455
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: June 11, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways