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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)DescriptionActionsGraphical viewLength
Binding sitei133NADPBy similarity1
Binding sitei153NADPBy similarity1
Binding sitei157FADBy similarity1
Binding sitei213FADBy similarity1
Binding sitei213NADP; via amide nitrogenBy similarity1
Binding sitei285NADPBy similarity1
Binding sitei352NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi130 – 133FADBy similarity4
Nucleotide bindingi151 – 153FADBy similarity3
Nucleotide bindingi172 – 174FADBy similarity3
Nucleotide bindingi245 – 246NADPBy similarity2
Nucleotide bindingi275 – 276NADPBy similarity2
Nucleotide bindingi313 – 314NADPBy similarity2

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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 35Chloroplast1 PublicationAdd BLAST35
ChainiPRO_000001940736 – 354Ferredoxin--NADP reductase, chloroplasticAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei118N6,N6,N6-trimethyllysine1 Publication1
Modified residuei124N6,N6,N6-trimethyllysine1 Publication1
Modified residuei170N6,N6-dimethyllysine1 Publication1

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP53991.
PRIDEiP53991.

Interactioni

Protein-protein interaction databases

DIPiDIP-58595N.
STRINGi3055.EDP00292.

Structurei

3D structure databases

ProteinModelPortaliP53991.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini69 – 198FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST130

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.
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...

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: October 5, 2016
This is version 97 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.