P10933 · FENR1_PEA
- ProteinFerredoxin--NADP reductase, leaf isozyme, chloroplastic
- GenePETH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids360 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Miscellaneous
FNR is probably attached to the membrane by a specific binding protein.
Catalytic activity
- H+ + NADP+ + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Cofactor
Pathway
Energy metabolism; photosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 139-142 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RLYS | ||||||
Binding site | 142 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 160-162 | FAD (UniProtKB | ChEBI) | ||||
Sequence: CVK | ||||||
Binding site | 162 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 166 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 177-179 | FAD (UniProtKB | ChEBI) | ||||
Sequence: VCS | ||||||
Binding site | 218 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 218 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 250-251 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VP | ||||||
Binding site | 280-281 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 290 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 319-320 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GL | ||||||
Binding site | 358 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | chloroplast thylakoid membrane | |
Molecular Function | ferredoxin-NADP+ reductase activity | |
Biological Process | photosynthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerredoxin--NADP reductase, leaf isozyme, chloroplastic
- EC number
- Short namesFNR
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum
Accessions
- Primary accessionP10933
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein
Note: In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 360 | Results in a 2.0-fold reduction in kcat for the diaphorase reaction. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 360 | Results in a 302-fold reduction in kcat for the diaphorase reaction. | ||||
Sequence: Y → G | ||||||
Mutagenesis | 360 | Results in a 22-fold reduction in kcat for the diaphorase reaction. | ||||
Sequence: Y → S | ||||||
Mutagenesis | 360 | Results in a 2.2-fold reduction in kcat for the diaphorase reaction. | ||||
Sequence: Y → W |
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-52 | Chloroplast | ||||
Sequence: MAAAVTAAVSLPYSNSTSLPIRTSIVAPERLVFKKVSLNNVSISGRVGTIRA | ||||||
Chain | PRO_0000019411 | 53-360 | Ferredoxin--NADP reductase, leaf isozyme, chloroplastic | |||
Sequence: QVTTEAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEVY |
Interaction
Subunit
Monomer. Interacts with TIC62 (via C-terminus).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P10933 | PETF P09911 | 3 | EBI-931306, EBI-931449 | |
BINARY | P10933 | TIC62 Q8SKU2 | 5 | EBI-931306, EBI-15606082 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 81-203 | FAD-binding FR-type | ||||
Sequence: KEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVPYREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLM |
Sequence similarities
Belongs to the ferredoxin--NADP reductase type 1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length360
- Mass (Da)40,194
- Last updated1989-07-01 v1
- Checksum7F1CC10DEBBA7B24
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X12446 EMBL· GenBank· DDBJ | CAA30978.1 EMBL· GenBank· DDBJ | mRNA | ||
L15565 EMBL· GenBank· DDBJ | AAB59349.1 EMBL· GenBank· DDBJ | mRNA | ||
L15567 EMBL· GenBank· DDBJ | AAB59303.1 EMBL· GenBank· DDBJ | mRNA | ||
L15569 EMBL· GenBank· DDBJ | AAB59304.1 EMBL· GenBank· DDBJ | mRNA |