P00455 (FENR_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferredoxin--NADP reductase, chloroplastic
Short name=FNR
EC=1.18.1.2

Gene names

Name:

PETH

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.
Cofactor	FAD.
Pathway	Energy metabolism; photosynthesis.
Subcellular location	Plastid › chloroplast stroma. Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Probable. Note: In the vicinity of the photosystem I in the non-stacked and fringe portion of the membrane.
Miscellaneous	FNR is probably attached to the membrane by a specific binding protein.
Sequence similarities	Belongs to the ferredoxin--NADP reductase type 1 family. Contains 1 FAD-binding FR-type domain.
Biophysicochemical properties	Kinetic parameters: KM=35 µM for NADPH Ref.5

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PETF	P00221	3	EBI-865079,EBI-864933

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 55

55

Chloroplast Ref.3

Chain

56 – 369

314

Ferredoxin--NADP reductase, chloroplastic

PRO_0000019412

Regions

Domain

90 – 212

123

FAD-binding FR-type

Nucleotide binding

148 – 151

4

FAD

Nucleotide binding

169 – 171

3

FAD

Nucleotide binding

186 – 188

3

FAD

Nucleotide binding

259 – 260

2

NADP

Nucleotide binding

289 – 290

2

NADP

Nucleotide binding

299 – 301

3

NADP

Nucleotide binding

328 – 329

2

NADP By similarity

Sites

Binding site

151

1

NADP By similarity

Binding site

171

1

NADP

Binding site

175

1

FAD

Binding site

227

1

FAD

Binding site

227

1

NADP; via amide nitrogen By similarity

Binding site

367

1

NADP By similarity

Natural variations

Natural variant

324

1

F → V.

Experimental info

Mutagenesis

367

1

E → A: Slightly reduced activity. Ref.6

Mutagenesis

367

1

E → D or Q: Reduced activity. Ref.6

Mutagenesis

367

1

E → L: Reduces activity by 99%. Ref.6

Secondary structure

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369

Helix Strand Turn

Details...

Beta strand

76 – 78

3

Beta strand

86 – 88

3

Beta strand

93 – 102

10

Beta strand

106 – 110

5

Beta strand

112 – 118

7

Beta strand

130 – 134

5

Beta strand

136 – 138

3

Beta strand

142 – 144

3

Beta strand

148 – 151

4

Beta strand

161 – 163

3

Beta strand

165 – 171

7

Beta strand

174 – 176

3

Beta strand

182 – 184

3

Helix

186 – 193

8

Beta strand

199 – 206

8

Beta strand

219 – 225

7

Helix

226 – 229

4

Helix

230 – 240

11

Beta strand

251 – 261

11

Helix

262 – 264

3

Helix

268 – 277

10

Turn

279 – 281

3

Beta strand

282 – 288

7

Turn

289 – 291

3

Helix

302 – 307

6

Helix

310 – 316

7

Beta strand

322 – 329

8

Helix

332 – 345

14

Turn

346 – 348

3

Helix

351 – 360

10

Beta strand

364 – 369

6

Sequences

	Sequence		Length	Mass (Da)
	P00455 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 1D0432BA47438A28	FASTA	369	41,188
	10 20 30 40 50 60 MTTAVTAAVS FPSTKTTSLS ARSSSVISPD KISYKKVPLY YRNVSATGKM GPIRAQIASD 70 80 90 100 110 120 VEAPPPAPAK VEKHSKKMEE GITVNKFKPK TPYVGRCLLN TKITGDDAPG ETWHMVFSHE 130 140 150 160 170 180 GEIPYREGQS VGVIPDGEDK NGKPHKLRLY SIASSALGDF GDAKSVSLCV KRLIYTNDAG 190 200 210 220 230 240 ETIKGVCSNF LCDLKPGAEV KLTGPVGKEM LMPKDPNATI IMLGTGTGIA PFRSFLWKMF 250 260 270 280 290 300 FEKHDDYKFN GLAWLFLGVP TSSSLLYKEE FEKMKEKAPD NFRLDFAVSR EQTNEKGEKM 310 320 330 340 350 360 YIQTRMAQYA VELWEMLKKD NTYFYMCGLK GMEKGIDDIM VSLAAAEGID WIEYKRQLKK AEQWNVEVY

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07981 mRNA. Translation: CAA30791.1.
M86349 mRNA. Translation: AAA34029.1.
X64351 Genomic DNA. Translation: CAA45703.1.

PIR

RDSPXX. S00438.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00455.

SMR

P00455. Positions 74-369.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00455. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P00455.

UniPathway

UPA00091.

Family and domain databases

InterPro

IPR017927. Fd_Rdtase_FAD-bd.
IPR015701. Fd_Red.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR012146. FNR.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

PANTHER

PTHR19384:SF1. PTHR19384:SF1. 1 hit.

Pfam

PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000361. Frd-NADP+_RD. 1 hit.

PRINTS

PR00371. FPNCR.

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00455.

Entry information

Entry name

FENR_SPIOL

Accession

Primary (citable) accession number: P00455

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1988
Last modified:	April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program