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Protein

Ferredoxin--NADP reductase, chloroplastic

Gene

PETH

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

Cofactori

Pathwayi: photosynthesis

This protein is involved in the pathway photosynthesis, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway photosynthesis and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331NADPBy similarity
Binding sitei153 – 1531NADPBy similarity
Binding sitei157 – 1571FADBy similarity
Binding sitei213 – 2131FADBy similarity
Binding sitei213 – 2131NADP; via amide nitrogenBy similarity
Binding sitei285 – 2851NADPBy similarity
Binding sitei352 – 3521NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi130 – 1334FADBy similarity
Nucleotide bindingi151 – 1533FADBy similarity
Nucleotide bindingi172 – 1743FADBy similarity
Nucleotide bindingi245 – 2462NADPBy similarity
Nucleotide bindingi275 – 2762NADPBy similarity
Nucleotide bindingi313 – 3142NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

UniPathwayiUPA00091.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin--NADP reductase, chloroplastic (EC:1.18.1.2)
Short name:
FNR
Gene namesi
Name:PETH
Synonyms:FNR
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Chloroplast1 PublicationAdd
BLAST
Chaini36 – 354319Ferredoxin--NADP reductase, chloroplasticPRO_0000019407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181N6,N6,N6-trimethyllysine1 Publication
Modified residuei124 – 1241N6,N6,N6-trimethyllysine1 Publication
Modified residuei170 – 1701N6,N6-dimethyllysine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP53991.
PRIDEiP53991.

Interactioni

Protein-protein interaction databases

DIPiDIP-58595N.
STRINGi3055.EDP00292.

Structurei

3D structure databases

ProteinModelPortaliP53991.
SMRiP53991. Positions 53-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 198130FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSiPR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53991-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLRKPSNH ADRACSRRLR VATRVAGRRM CRPVAATKAS TAVTTDMSKR
60 70 80 90 100
TVPTKLEEGE MPLNTYSNKA PFKAKVRSVE KITGPKATGE TCHIIIETEG
110 120 130 140 150
KIPFWEGQSY GVIPPGTKIN SKGKEVPTAR LYSIASSRYG DDGDGQTASL
160 170 180 190 200
CVRRAVYVDP ETGKEDPAKK GLCSNFLCDA TPGTEISMTG PTGKVLLLPA
210 220 230 240 250
DANAPLICVA TGTGIAPFRS FWRRCFIENV PSYKFTGLFW LFMGVGNSDA
260 270 280 290 300
KLYDEELQAI AKAYPGQFRL DYALSREQNN RKGGKMYIQD KVEEYADEIF
310 320 330 340 350
DLLDNGAHMY FCGLKGMMPG IQDMLERVAK EKGLNYEEWV EGLKHKNQWH

VEVY
Length:354
Mass (Da):39,277
Last modified:October 1, 1996 - v1
Checksum:i4927FBA0CF668FBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10545 mRNA. Translation: AAA79131.1.
PIRiT08035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10545 mRNA. Translation: AAA79131.1.
PIRiT08035.

3D structure databases

ProteinModelPortaliP53991.
SMRiP53991. Positions 53-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58595N.
STRINGi3055.EDP00292.

Proteomic databases

PaxDbiP53991.
PRIDEiP53991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00091.

Family and domain databases

InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015701. FNR.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000361. Frd-NADP+_RD. 1 hit.
PRINTSiPR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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.

Entry informationi

Entry nameiFENR_CHLRE
AccessioniPrimary (citable) accession number: P53991
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.