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P00455

- FENR_SPIOL

UniProt

P00455 - FENR_SPIOL

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Protein

Ferredoxin--NADP reductase, chloroplastic

Gene

PETH

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - 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

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

GO - Biological processi

  1. photosynthesis Source: UniProtKB-UniPathway
Complete GO annotation...

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 Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
  3. thylakoid Source: UniProtKB-KW
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 .
PIRi S00438. RDSPXX.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 116 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