Q6ZFJ3 · FENR2_ORYSJ
- ProteinFerredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- GeneLFNR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids366 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Plays 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
- 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 | 145-148 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RLYS | ||||||
Binding site | 148 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 166-168 | FAD (UniProtKB | ChEBI) | ||||
Sequence: CVK | ||||||
Binding site | 168 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 172 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 183-185 | FAD (UniProtKB | ChEBI) | ||||
Sequence: VCS | ||||||
Binding site | 224 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 224 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 256-257 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: VP | ||||||
Binding site | 286-287 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 296 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 325-326 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GL | ||||||
Binding site | 364 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast stroma | |
Cellular Component | chloroplast thylakoid membrane protein complex | |
Molecular Function | electron transfer activity | |
Molecular Function | ferredoxin-NADP+ reductase activity | |
Biological Process | electron transport chain | |
Biological Process | photosynthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ6ZFJ3
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-48 | Chloroplast | ||||
Sequence: MAAVNTVSSLPCSKAGAAVAGGAPRPSTCSVFYPPRCWSKRSSGNGVR | ||||||
Chain | PRO_0000442379 | 49-366 | Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic | |||
Sequence: AQASTTETTAAPAAEVTTKVEKVSKKQVDGVVTNKYRPKEPYTGRCLLNTRITGDDAPGETWHMVFSTDGEIPYREGQSIGVIPDGIDKNGKPHKLRLYSIASSAIGDFADSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGSDVKITGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEEHDDYKFNGLAWLFLGVPTSSTLLYREEFERMKEIAPERFRLDFAVSREQTNAAGEKMYIQTRMAEYKDELWELLKKDNTYVYMCGLKGMEKGIDDIMIDLAAKDGIDWLDYKKQLKKSEQWNVEVY | ||||||
Disulfide bond | 184↔189 | |||||
Sequence: CSNFLC | ||||||
Modified residue | 185 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 216 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
May form interchain disulfide bonds with LIR1.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Heterodimer with LFNR1 (By similarity).
Component of high molecular weight thylakoid LFNRs-containing protein complexes containing LIR1, LFNR1, LFNR2, TIC62 and TROL proteins. Interacts directly with LIR1 and TIC62; LIR1 increases the affinity of LFNR1 and LFNR2 for TIC62 (PubMed:26941088).
Component of high molecular weight thylakoid LFNRs-containing protein complexes containing LIR1, LFNR1, LFNR2, TIC62 and TROL proteins. Interacts directly with LIR1 and TIC62; LIR1 increases the affinity of LFNR1 and LFNR2 for TIC62 (PubMed:26941088).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 87-209 | FAD-binding FR-type | ||||
Sequence: KEPYTGRCLLNTRITGDDAPGETWHMVFSTDGEIPYREGQSIGVIPDGIDKNGKPHKLRLYSIASSAIGDFADSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGSDVKITGPVGKEMLM |
Sequence similarities
Belongs to the ferredoxin--NADP reductase type 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length366
- Mass (Da)40,665
- Last updated2004-07-05 v1
- Checksum01C5BCE33EF30F09
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q6ZFJ4 | Q6ZFJ4_ORYSJ | Os02g0103800 | 350 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP004187 EMBL· GenBank· DDBJ | BAD07827.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014958 EMBL· GenBank· DDBJ | BAS76543.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000139 EMBL· GenBank· DDBJ | EAZ21407.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK065309 EMBL· GenBank· DDBJ | BAG89459.1 EMBL· GenBank· DDBJ | mRNA |