Skip Header

Contribute Send feedback
Read comments (?) or add your own

P10933 (FENR1_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. 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
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, leaf isozyme, chloroplastic
Short name=FNR
EC=1.18.1.2
Gene names
Name:PETH
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length360 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.

Subunit structure

Monomer. Interacts with TIC62 (via C-terminus). Ref.3

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.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PETFP099113EBI-931306,EBI-931449

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Chloroplast
Chain53 – 360308Ferredoxin--NADP reductase, leaf isozyme, chloroplastic
PRO_0000019411

Regions

Domain81 – 203123FAD-binding FR-type
Nucleotide binding139 – 1424FAD
Nucleotide binding160 – 1623FAD
Nucleotide binding177 – 1793FAD
Nucleotide binding250 – 2512NADP
Nucleotide binding280 – 2812NADP
Nucleotide binding319 – 3202NADP

Sites

Binding site1421NADP
Binding site1621NADP
Binding site1661FAD
Binding site2181FAD By similarity
Binding site2181NADP; via amide nitrogen
Binding site2901NADP
Binding site3581NADP

Experimental info

Mutagenesis3601Y → F: Results in a 2.0-fold reduction in kcat for the diaphorase reaction. Ref.2
Mutagenesis3601Y → G: Results in a 302-fold reduction in kcat for the diaphorase reaction. Ref.2
Mutagenesis3601Y → S: Results in a 22-fold reduction in kcat for the diaphorase reaction. Ref.2
Mutagenesis3601Y → W: Results in a 2.2-fold reduction in kcat for the diaphorase reaction. Ref.2

Secondary structure

1 ........................................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10933 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 7F1CC10DEBBA7B24

FASTA36040,194
        10         20         30         40         50         60 
MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNN VSISGRVGTI RAQVTTEAPA 

        70         80         90        100        110        120 
KVVKHSKKQD ENIVVNKFKP KEPYVGRCLL NTKITGDDAP GETWHMVFST EGEVPYREGQ 

       130        140        150        160        170        180 
SIGIVPDGID KNGKPHKLRL YSIASSAIGD FGDSKTVSLC VKRLVYTNDA GEVVKGVCSN 

       190        200        210        220        230        240 
FLCDLKPGSE VKITGPVGKE MLMPKDPNAT VIMLGTGTGI APFRSFLWKM FFEKHEDYQF 

       250        260        270        280        290        300 
NGLAWLFLGV PTSSSLLYKE EFEKMKEKAP ENFRLDFAVS REQVNDKGEK MYIQTRMAQY 

       310        320        330        340        350        360 
AEELWELLKK DNTFVYMCGL KGMEKGIDDI MVSLAAKDGI DWIEYKRTLK KAEQWNVEVY

« Hide

References

[1]"Characterisation of a full-length cDNA clone for pea ferredoxin-NADP+ reductase."
Newman B.J., Gray J.C.
Plant Mol. Biol. 10:511-520(1988) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Little Marvel.
Tissue: Leaf.
[2]"Probing the role of the carboxyl-terminal region of ferredoxin-NADP+ reductase by site-directed mutagenesis and deletion analysis."
Orellano E.G., Calcaterra N.B., Carrillo N., Ceccarelli E.A.
J. Biol. Chem. 268:19267-19273(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 270-360, MUTAGENESIS OF TYR-360.
[3]"Protein import into chloroplasts involves redox-regulated proteins."
Kuechler M., Decker S., Hoermann F., Soll J., Heins L.
EMBO J. 21:6136-6145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIC62.
[4]"A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies."
Deng Z., Aliverti A., Zanetti G., Arakaki A.K., Ottado J., Orellano E.G., Calcaterra N.B., Ceccarelli E.A., Carrillo N., Karplus P.A.
Nat. Struct. Biol. 6:847-853(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD AND NADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X12446 mRNA. Translation: CAA30978.1.
L15565 mRNA. Translation: AAB59349.1.
L15567 mRNA. Translation: AAB59303.1.
L15569 mRNA. Translation: AAB59304.1.
PIRS04030.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFYX-ray1.80A/B53-359[»]
1QFZX-ray1.70A/B53-359[»]
1QG0X-ray2.50A/B53-360[»]
1QGAX-ray2.00A/B53-359[»]
2XNCX-ray2.90A/B51-360[»]
3MHPX-ray1.70A/B66-360[»]
4AF6X-ray2.90A/B53-360[»]
4AF7X-ray2.85A/B53-360[»]
ProteinModelPortalP10933.
SMRP10933. Positions 53-359.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35575N.
IntActP10933. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00091.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR015701. Fd_Red.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR19384:SF1. PTHR19384:SF1. 1 hit.
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10933.

Entry information

Entry nameFENR1_PEA
AccessionPrimary (citable) accession number: P10933
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents