Q9FKW6 · FNRL1_ARATH
- ProteinFerredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- GeneLFNR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids360 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (PubMed:17335513, Ref.7). Probable electron donor required for the MgProto monomethylester (MgProtoME) cyclase complex reaction to form protochlorophyllide, thus connecting chlorophyll synthesis with photosynthetic activity (PubMed:29443418).
Catalytic activity
- 2 reduced [2Fe-2S]-[ferredoxin] + NADP+ + H+ = 2 oxidized [2Fe-2S]-[ferredoxin] + NADPH
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.5 μM | ferredoxin-1 | |||||
2.5 μM | ferredoxin-2 | |||||
4.6 μM | ferredoxin-3 |
Pathway
Energy metabolism; photosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 139-142 | FAD (UniProtKB | ChEBI) | |||
Binding site | 142 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 160-162 | FAD (UniProtKB | ChEBI) | |||
Binding site | 162 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 166 | FAD (UniProtKB | ChEBI) | |||
Binding site | 177-179 | FAD (UniProtKB | ChEBI) | |||
Binding site | 218 | FAD (UniProtKB | ChEBI) | |||
Binding site | 218 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 250-251 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 280-281 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 290 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 319-320 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 358 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apoplast | |
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast stroma | |
Cellular Component | chloroplast thylakoid | |
Cellular Component | chloroplast thylakoid membrane | |
Cellular Component | chloroplast thylakoid membrane protein complex | |
Cellular Component | plastid | |
Cellular Component | thylakoid | |
Cellular Component | thylakoid lumen | |
Molecular Function | electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity | |
Molecular Function | electron transporter, transferring electrons within the noncyclic electron transport pathway of photosynthesis activity | |
Molecular Function | ferredoxin-NADP+ reductase activity | |
Molecular Function | poly(U) RNA binding | |
Molecular Function | protein domain specific binding | |
Biological Process | photosynthetic electron transport chain | |
Biological Process | regulation of tetrapyrrole biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFerredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FKW6
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein
Note: More abundant in the membrane fraction.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Plants have a reduced capacity for carbon fixation and prevent the association of LFNR2 with the thylakoid membrane (PubMed:17335513).
Accumulation of MgProto monomethylester (MgProtoME) but altered tetrapyrrole biosynthesis (TBS) associated with reduced YCF54 levels and lower MgProtoME cyclase activity (PubMed:29443418).
Accumulation of MgProto monomethylester (MgProtoME) but altered tetrapyrrole biosynthesis (TBS) associated with reduced YCF54 levels and lower MgProtoME cyclase activity (PubMed:29443418).
Variants
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We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 9 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-49 | Chloroplast | |||
Chain | PRO_0000322572 | 50-360 | Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic | ||
Disulfide bond | 178↔183 | ||||
Modified residue | 179 | Phosphoserine | |||
Modified residue | 210 | Phosphothreonine | |||
Post-translational modification
May form interchain disulfide bonds with LIR1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in shoots. Restricted to green tissues, being more abundant in siliques.
Induction
By nitrate.
Gene expression databases
Interaction
Subunit
Heterodimer with LFNR2. Interacts with PGRL1A and PGRL1B. Interacts with TIC62. 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 (By similarity).
Binds to YCF54 in chloroplasts (PubMed:29443418).
Binds to YCF54 in chloroplasts (PubMed:29443418).
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 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.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q9FKW6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length360
- Mass (Da)40,326
- Last updated2001-03-01 v1
- MD5 ChecksumD3E1D2DF0116693EA660CC4D5EEB3F34
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JZ46 | F4JZ46_ARATH | FNR1 | 262 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 5; BAE98556 | |||
Sequence conflict | 113 | in Ref. 1; CAB52472 | |||
Sequence conflict | 276-278 | in Ref. 1; CAB52472 | |||
Sequence conflict | 292 | in Ref. 1; CAB52472 | |||
Sequence conflict | 345 | in Ref. 1; CAB52472 | |||
Sequence conflict | 360 | in Ref. 1; CAB52472 | |||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ243705 EMBL· GenBank· DDBJ | CAB52472.1 EMBL· GenBank· DDBJ | mRNA | ||
AB011474 EMBL· GenBank· DDBJ | BAB10424.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED98174.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY072112 EMBL· GenBank· DDBJ | AAL59934.1 EMBL· GenBank· DDBJ | mRNA | ||
AY096665 EMBL· GenBank· DDBJ | AAM20299.1 EMBL· GenBank· DDBJ | mRNA | ||
AK226411 EMBL· GenBank· DDBJ | BAE98556.1 EMBL· GenBank· DDBJ | mRNA |