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Reviewed, UniProtKB/Swiss-Prot P53991 (FENR_CHLRE)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ferredoxin--NADP reductase, chloroplastic
      Short name=FNR
    EC=1.18.1.2
Gene names
Name: PETH
Synonyms: FNR
OrganismChlamydomonas reinhardtii
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

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Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Contains 1 FAD-binding FR-type domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Chloroplast Ref.2
Chain36 – 354319Ferredoxin--NADP reductase, chloroplastic
PRO_0000019407

Regions

Domain69 – 198130FAD-binding FR-type
Nucleotide binding130 – 1334FAD By similarity
Nucleotide binding151 – 1533FAD By similarity
Nucleotide binding172 – 1743FAD By similarity
Nucleotide binding245 – 2462NADP By similarity
Nucleotide binding275 – 2762NADP By similarity
Nucleotide binding313 – 3142NADP By similarity

Sites

Binding site1331NADP By similarity
Binding site1531NADP By similarity
Binding site1571FAD By similarity
Binding site2131FAD By similarity
Binding site2131NADP; via amide nitrogen By similarity
Binding site2851NADP By similarity
Binding site3521NADP By similarity

Amino acid modifications

Modified residue1181N6,N6,N6-trimethyllysine Ref.2
Modified residue1241N6,N6,N6-trimethyllysine Ref.2
Modified residue1701N6,N6-dimethyllysine Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P53991-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4927FBA0CF668FBD

FASTA35439,277
        10         20         30         40         50         60 
MASLRKPSNH ADRACSRRLR VATRVAGRRM CRPVAATKAS TAVTTDMSKR TVPTKLEEGE 

        70         80         90        100        110        120 
MPLNTYSNKA PFKAKVRSVE KITGPKATGE TCHIIIETEG KIPFWEGQSY GVIPPGTKIN 

       130        140        150        160        170        180 
SKGKEVPTAR LYSIASSRYG DDGDGQTASL CVRRAVYVDP ETGKEDPAKK GLCSNFLCDA 

       190        200        210        220        230        240 
TPGTEISMTG PTGKVLLLPA DANAPLICVA TGTGIAPFRS FWRRCFIENV PSYKFTGLFW 

       250        260        270        280        290        300 
LFMGVGNSDA KLYDEELQAI AKAYPGQFRL DYALSREQNN RKGGKMYIQD KVEEYADEIF 

       310        320        330        340        350 
DLLDNGAHMY FCGLKGMMPG IQDMLERVAK EKGLNYEEWV EGLKHKNQWH VEVY

« Hide

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References

[1]"A cDNA clone encoding a ferredoxin-NADP+ reductase from Chlamydomonas reinhardtii."
Kitayama M., Kitayama K., Togasaki R.K.
Plant Physiol. 106:1715-1716(1994) [PubMed: 7846183] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Specific post-translational methylation of three lysine residues in Chlamydomonas reinhardtii ferredoxin-NADP reductase."
Decottignies P., Flesch V., Jacquot J.-P., Schmitter J.-M., le Marechal P.
(In) Proceedings of XIth international conference on methods in protein structure analysis, pp.45-45, Annecy (1996)
Cited for: PROTEIN SEQUENCE OF 36-265, METHYLATION AT LYS-118; LYS-124 AND LYS-170.

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Cross-references

Sequence databases

U10545 mRNA. Translation: AAA79131.1.
PIRT08035.

3D structure databases

HSSPHSSP built from PDB template 1JB9 based on UniProtKB Q41736.
ModBaseSearch...

Proteomic databases

PRIDEP53991.

Enzyme and pathway databases

BRENDA1.18.1.2. 144.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. Frd-NADP+_RD.
IPR015701. FRD_Red.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PANTHERPTHR19384:SF1. FRD_Red. 1 hit.
PfamPF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSPR00371. FPNCR.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFENR_CHLRE
AccessionPrimary (citable) accession number: P53991
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents