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P00455

- FENR_SPIOL

UniProt

P00455 - FENR_SPIOL

Protein

Ferredoxin--NADP reductase, chloroplastic

Gene

PETH

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    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

    FAD.

    Kineticsi

    1. KM=35 µM for NADPH1 Publication

    Pathwayi

    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

    1. ferredoxin-NADP+ reductase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    GO - Biological processi

    1. photosynthesis Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Photosynthesis, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    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

    Plastidchloroplast stroma. Plastidchloroplast thylakoid membrane Curated; Peripheral membrane protein Curated; Stromal side Curated
    Note: In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane.

    GO - Cellular componenti

    1. chloroplast stroma Source: UniProtKB-SubCell
    2. chloroplast thylakoid membrane Source: UniProtKB-SubCell

    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 – 783
    Beta strandi86 – 883
    Beta strandi93 – 10210
    Beta strandi106 – 1105
    Beta strandi112 – 1187
    Beta strandi130 – 1345
    Beta strandi136 – 1383
    Beta strandi142 – 1443
    Beta strandi148 – 1514
    Beta strandi161 – 1633
    Beta strandi165 – 1717
    Beta strandi174 – 1763
    Beta strandi182 – 1843
    Helixi186 – 1938
    Beta strandi199 – 2068
    Beta strandi219 – 2257
    Helixi226 – 2294
    Helixi230 – 24011
    Beta strandi251 – 26111
    Helixi262 – 2643
    Helixi268 – 27710
    Turni279 – 2813
    Beta strandi282 – 2887
    Turni289 – 2913
    Helixi302 – 3076
    Helixi310 – 3167
    Beta strandi322 – 3298
    Helixi332 – 34514
    Turni346 – 3483
    Helixi351 – 36010
    Beta strandi364 – 3696

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MTTAVTAAVS FPSTKTTSLS ARSSSVISPD KISYKKVPLY YRNVSATGKM    50
    GPIRAQIASD VEAPPPAPAK VEKHSKKMEE GITVNKFKPK TPYVGRCLLN 100
    TKITGDDAPG ETWHMVFSHE GEIPYREGQS VGVIPDGEDK NGKPHKLRLY 150
    SIASSALGDF GDAKSVSLCV KRLIYTNDAG ETIKGVCSNF LCDLKPGAEV 200
    KLTGPVGKEM LMPKDPNATI IMLGTGTGIA PFRSFLWKMF FEKHDDYKFN 250
    GLAWLFLGVP TSSSLLYKEE FEKMKEKAPD NFRLDFAVSR EQTNEKGEKM 300
    YIQTRMAQYA VELWEMLKKD NTYFYMCGLK GMEKGIDDIM VSLAAAEGID 350
    WIEYKRQLKK AEQWNVEVY 369
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07981 mRNA. Translation: CAA30791.1 .
    M86349 mRNA. Translation: AAA34029.1 .
    X64351 Genomic DNA. Translation: CAA45703.1 .
    PIRi S00438. RDSPXX.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BX0 X-ray 1.90 A 56-369 [» ]
    1BX1 X-ray 1.90 A 56-369 [» ]
    1FNB X-ray 1.70 A 56-369 [» ]
    1FNC X-ray 2.00 A 56-369 [» ]
    1FND X-ray 1.70 A 56-369 [» ]
    1FRN X-ray 2.00 A 56-369 [» ]
    1FRQ X-ray 1.95 A 56-369 [» ]
    ProteinModelPortali P00455.
    SMRi P00455. Positions 74-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00455. 2 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00091 .
    SABIO-RK P00455.

    Miscellaneous databases

    EvolutionaryTracei P00455.

    Family and domain databases

    InterProi IPR017927. 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 ]
    Pfami PF00970. FAD_binding_6. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000361. Frd-NADP+_RD. 1 hit.
    PRINTSi PR00371. FPNCR.
    SUPFAMi SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 114 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