Q9FKW6 · FNRL1_ARATH

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

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
3.5 μMferredoxin-1
2.5 μMferredoxin-2
4.6 μMferredoxin-3

Pathway

Energy metabolism; photosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site139-142FAD (UniProtKB | ChEBI)
Binding site142NADP+ (UniProtKB | ChEBI)
Binding site160-162FAD (UniProtKB | ChEBI)
Binding site162NADP+ (UniProtKB | ChEBI)
Binding site166FAD (UniProtKB | ChEBI)
Binding site177-179FAD (UniProtKB | ChEBI)
Binding site218FAD (UniProtKB | ChEBI)
Binding site218NADP+ (UniProtKB | ChEBI)
Binding site250-251NADP+ (UniProtKB | ChEBI)
Binding site280-281NADP+ (UniProtKB | ChEBI)
Binding site290NADP+ (UniProtKB | ChEBI)
Binding site319-320NADP+ (UniProtKB | ChEBI)
Binding site358NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentapoplast
Cellular Componentchloroplast
Cellular Componentchloroplast envelope
Cellular Componentchloroplast stroma
Cellular Componentchloroplast thylakoid
Cellular Componentchloroplast thylakoid membrane
Cellular Componentchloroplast thylakoid membrane protein complex
Cellular Componentplastid
Cellular Componentthylakoid
Cellular Componentthylakoid lumen
Molecular Functionelectron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity
Molecular Functionelectron transporter, transferring electrons within the noncyclic electron transport pathway of photosynthesis activity
Molecular Functionferredoxin-NADP+ reductase activity
Molecular Functionpoly(U) RNA binding
Molecular Functionprotein domain specific binding
Biological Processphotosynthetic electron transport chain
Biological Processregulation of tetrapyrrole biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
  • EC number
  • Alternative names
    • Leaf FNR 1
      (AtLFNR1
      ; FNR-1
      )

Gene names

    • Name
      LFNR1
    • Synonyms
      PETH1
    • ORF names
      K2A18.27
    • Ordered locus names
      At5g66190

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FKW6
  • Secondary accessions
    • Q0WWE2
    • Q9SUJ3

Proteomes

Organism-specific databases

Genome annotation databases

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).

Variants

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.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain, disulfide bond, modified residue.

Type
IDPosition(s)Description
Transit peptide1-49Chloroplast
ChainPRO_000032257250-360Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
Disulfide bond178↔183
Modified residue179Phosphoserine
Modified residue210Phosphothreonine

Post-translational modification

May form interchain disulfide bonds with LIR1.

Keywords

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).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain81-203FAD-binding FR-type

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Length
    360
  • Mass (Da)
    40,326
  • Last updated
    2001-03-01 v1
  • MD5 Checksum
    D3E1D2DF0116693EA660CC4D5EEB3F34
MAAAISAAVSLPSSKSSSLLTKISSVSPQRIFLKKSTVCYRRVVSVKAQVTTDTTEAPPVKVVKESKKQEEGIVVNKFKPKNPYTGRCLLNTKITGDDAPGETWHIVFTTEGEVPYREGQSIGVIPEGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDGGEIVKGVCSNFLCDLKPGDEAKITGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEEHEDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKNPDNFRLDFAVSREQTNEKGEKMYIQTRMAEYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWLEYKKQLKRSEQWNVEVY

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4JZ46F4JZ46_ARATHFNR1262

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 5; BAE98556
Sequence conflict113in Ref. 1; CAB52472
Sequence conflict276-278in Ref. 1; CAB52472
Sequence conflict292in Ref. 1; CAB52472
Sequence conflict345in Ref. 1; CAB52472
Sequence conflict360in Ref. 1; CAB52472

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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