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Protein

Ferredoxin--NADP reductase, chloroplastic

Gene

PETH

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 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

Kineticsi

  1. KM=35 µM for NADPH1 Publication

    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 sitei151NADPBy similarity1
    Binding sitei171NADP1
    Binding sitei175FAD2 Publications1
    Binding sitei227FAD2 Publications1
    Binding sitei227NADP; via amide nitrogenBy similarity1
    Binding sitei367NADPBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi148 – 151FAD2 Publications4
    Nucleotide bindingi169 – 171FAD2 Publications3
    Nucleotide bindingi186 – 188FAD2 Publications3
    Nucleotide bindingi259 – 260NADP2
    Nucleotide bindingi289 – 290NADP2
    Nucleotide bindingi299 – 301NADP3
    Nucleotide bindingi328 – 329NADPBy 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

    BRENDAi1.18.1.2. 5812.
    SABIO-RKP00455.
    UniPathwayiUPA00091.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferredoxin--NADP reductase, chloroplastic (EC:1.18.1.2)
    Short name:
    FNR
    Gene namesi
    Name:PETH
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Thylakoid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi367E → A: Slightly reduced activity. 1 Publication1
    Mutagenesisi367E → D or Q: Reduced activity. 1 Publication1
    Mutagenesisi367E → L: Reduces activity by 99%. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 55Chloroplast1 PublicationAdd BLAST55
    ChainiPRO_000001941256 – 369Ferredoxin--NADP reductase, chloroplasticAdd BLAST314

    Proteomic databases

    PRIDEiP00455.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PETFP002213EBI-865079,EBI-864933

    Protein-protein interaction databases

    IntActiP00455. 2 interactors.

    Structurei

    Secondary structure

    1369
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi76 – 78Combined sources3
    Beta strandi86 – 88Combined sources3
    Beta strandi93 – 102Combined sources10
    Beta strandi106 – 110Combined sources5
    Beta strandi112 – 118Combined sources7
    Beta strandi130 – 134Combined sources5
    Beta strandi136 – 138Combined sources3
    Beta strandi142 – 144Combined sources3
    Beta strandi148 – 151Combined sources4
    Beta strandi161 – 163Combined sources3
    Beta strandi165 – 171Combined sources7
    Beta strandi174 – 176Combined sources3
    Beta strandi182 – 184Combined sources3
    Helixi186 – 193Combined sources8
    Beta strandi199 – 206Combined sources8
    Beta strandi219 – 225Combined sources7
    Helixi226 – 229Combined sources4
    Helixi230 – 240Combined sources11
    Beta strandi251 – 261Combined sources11
    Helixi262 – 264Combined sources3
    Helixi268 – 277Combined sources10
    Turni279 – 281Combined sources3
    Beta strandi282 – 288Combined sources7
    Turni289 – 291Combined sources3
    Helixi302 – 307Combined sources6
    Helixi310 – 316Combined sources7
    Beta strandi322 – 329Combined sources8
    Helixi332 – 345Combined sources14
    Turni346 – 348Combined sources3
    Helixi351 – 360Combined sources10
    Beta strandi364 – 369Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BX0X-ray1.90A56-369[»]
    1BX1X-ray1.90A56-369[»]
    1FNBX-ray1.70A56-369[»]
    1FNCX-ray2.00A56-369[»]
    1FNDX-ray1.70A56-369[»]
    1FRNX-ray2.00A56-369[»]
    1FRQX-ray1.95A56-369[»]
    ProteinModelPortaliP00455.
    SMRiP00455.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00455.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini90 – 212FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST123

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK02641.

    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.

    P00455-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTAVTAAVS FPSTKTTSLS ARSSSVISPD KISYKKVPLY YRNVSATGKM
    60 70 80 90 100
    GPIRAQIASD VEAPPPAPAK VEKHSKKMEE GITVNKFKPK TPYVGRCLLN
    110 120 130 140 150
    TKITGDDAPG ETWHMVFSHE GEIPYREGQS VGVIPDGEDK NGKPHKLRLY
    160 170 180 190 200
    SIASSALGDF GDAKSVSLCV KRLIYTNDAG ETIKGVCSNF LCDLKPGAEV
    210 220 230 240 250
    KLTGPVGKEM LMPKDPNATI IMLGTGTGIA PFRSFLWKMF FEKHDDYKFN
    260 270 280 290 300
    GLAWLFLGVP TSSSLLYKEE FEKMKEKAPD NFRLDFAVSR EQTNEKGEKM
    310 320 330 340 350
    YIQTRMAQYA VELWEMLKKD NTYFYMCGLK GMEKGIDDIM VSLAAAEGID
    360
    WIEYKRQLKK AEQWNVEVY
    Length:369
    Mass (Da):41,188
    Last modified:November 1, 1988 - v1
    Checksum:i1D0432BA47438A28
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural varianti324F → V.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X07981 mRNA. Translation: CAA30791.1.
    M86349 mRNA. Translation: AAA34029.1.
    X64351 Genomic DNA. Translation: CAA45703.1.
    PIRiS00438. RDSPXX.

    Genome annotation databases

    KEGGiag:CAA30791.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X07981 mRNA. Translation: CAA30791.1.
    M86349 mRNA. Translation: AAA34029.1.
    X64351 Genomic DNA. Translation: CAA45703.1.
    PIRiS00438. RDSPXX.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BX0X-ray1.90A56-369[»]
    1BX1X-ray1.90A56-369[»]
    1FNBX-ray1.70A56-369[»]
    1FNCX-ray2.00A56-369[»]
    1FNDX-ray1.70A56-369[»]
    1FRNX-ray2.00A56-369[»]
    1FRQX-ray1.95A56-369[»]
    ProteinModelPortaliP00455.
    SMRiP00455.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP00455. 2 interactors.

    Proteomic databases

    PRIDEiP00455.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA30791.

    Phylogenomic databases

    KOiK02641.

    Enzyme and pathway databases

    UniPathwayiUPA00091.
    BRENDAi1.18.1.2. 5812.
    SABIO-RKP00455.

    Miscellaneous databases

    EvolutionaryTraceiP00455.

    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_SPIOL
    AccessioniPrimary (citable) accession number: P00455
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1988
    Last modified: November 2, 2016
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    FNR is probably attached to the membrane by a specific binding protein.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.