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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

    Pathway: 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 sitei151 – 1511NADPBy similarity
    Binding sitei171 – 1711NADP
    Binding sitei175 – 1751FAD2 Publications
    Binding sitei227 – 2271FAD2 Publications
    Binding sitei227 – 2271NADP; via amide nitrogenBy similarity
    Binding sitei367 – 3671NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi148 – 1514FAD2 Publications
    Nucleotide bindingi169 – 1713FAD2 Publications
    Nucleotide bindingi186 – 1883FAD2 Publications
    Nucleotide bindingi259 – 2602NADP
    Nucleotide bindingi289 – 2902NADP
    Nucleotide bindingi299 – 3013NADP
    Nucleotide bindingi328 – 3292NADPBy 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

    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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Thylakoid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi367 – 3671E → A: Slightly reduced activity. 1 Publication
    Mutagenesisi367 – 3671E → D or Q: Reduced activity. 1 Publication
    Mutagenesisi367 – 3671E → L: Reduces activity by 99%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5555Chloroplast1 PublicationAdd
    BLAST
    Chaini56 – 369314Ferredoxin--NADP reductase, chloroplasticPRO_0000019412Add
    BLAST

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

    IntActiP00455. 2 interactions.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi76 – 783Combined sources
    Beta strandi86 – 883Combined sources
    Beta strandi93 – 10210Combined sources
    Beta strandi106 – 1105Combined sources
    Beta strandi112 – 1187Combined sources
    Beta strandi130 – 1345Combined sources
    Beta strandi136 – 1383Combined sources
    Beta strandi142 – 1443Combined sources
    Beta strandi148 – 1514Combined sources
    Beta strandi161 – 1633Combined sources
    Beta strandi165 – 1717Combined sources
    Beta strandi174 – 1763Combined sources
    Beta strandi182 – 1843Combined sources
    Helixi186 – 1938Combined sources
    Beta strandi199 – 2068Combined sources
    Beta strandi219 – 2257Combined sources
    Helixi226 – 2294Combined sources
    Helixi230 – 24011Combined sources
    Beta strandi251 – 26111Combined sources
    Helixi262 – 2643Combined sources
    Helixi268 – 27710Combined sources
    Turni279 – 2813Combined sources
    Beta strandi282 – 2887Combined sources
    Turni289 – 2913Combined sources
    Helixi302 – 3076Combined sources
    Helixi310 – 3167Combined sources
    Beta strandi322 – 3298Combined sources
    Helixi332 – 34514Combined sources
    Turni346 – 3483Combined sources
    Helixi351 – 36010Combined sources
    Beta strandi364 – 3696Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 74-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00455.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 212123FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    InterProiIPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR015701. FNR.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00970. FAD_binding_6. 1 hit.
    PF00175. 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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241F → V.

    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.

    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
    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. Positions 74-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP00455. 2 interactions.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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.
    IPR008333. OxRdtase_FAD-bd_dom.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00970. FAD_binding_6. 1 hit.
    PF00175. 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. "Analysis of cDNA clones encoding the entire precursor-polypeptide for ferredoxin:NADP+ oxidoreductase from spinach."
      Jansen T., Reilaender H., Steppuhn J., Herrmann R.G.
      Curr. Genet. 13:517-522(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and sequencing of the cDNA for precursor ferredoxin-NADP+: oxidoreductase from spinach."
      Alter J.M., Patrie W.J.
      Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase."
      Karplus P.A., Walsh K.A., Herriott J.R.
      Biochemistry 23:6576-6583(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 56-369.
    4. "Characterization of the promoter from the single-copy gene encoding ferredoxin-NADP(+)-oxidoreductase from spinach."
      Oelmueller R., Bolle C., Tyagi A.K., Niekrawietz N., Breit S.
      Mol. Gen. Genet. 237:261-272(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
    5. "Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family."
      Karplus P.A., Daniels M.J., Herriott J.R.
      Science 251:60-66(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND 2-PHOSPHO-AMP, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase."
      Aliverti A., Deng Z., Ravasi D., Piubelli L., Karplus P.A., Zanetti G.
      J. Biol. Chem. 273:34008-34015(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-369 OF MUTANTS ALA/GLN/LEU-367 IN COMPLEX WITH FAD, MUTAGENESIS OF GLU-367.
      Tissue: Leaf.

    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: April 1, 2015
    This is version 118 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

    External Data

    Dasty 3

    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 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.