P10933 (FENR1_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

PETH

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	360 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.
Subunit structure	Monomer. Interacts with TIC62 (via C-terminus). Ref.3
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.

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
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PETF	P09911	3	EBI-931306,EBI-931449

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 52

52

Chloroplast

Chain

53 – 360

308

Ferredoxin--NADP reductase, leaf isozyme, chloroplastic

PRO_0000019411

Regions

Domain

81 – 203

123

FAD-binding FR-type

Nucleotide binding

139 – 142

4

FAD

Nucleotide binding

160 – 162

3

FAD

Nucleotide binding

177 – 179

3

FAD

Nucleotide binding

250 – 251

2

NADP

Nucleotide binding

280 – 281

2

NADP

Nucleotide binding

319 – 320

2

NADP

Sites

Binding site

142

1

NADP

Binding site

162

1

NADP

Binding site

166

1

FAD

Binding site

218

1

FAD By similarity

Binding site

218

1

NADP; via amide nitrogen

Binding site

290

1

NADP

Binding site

358

1

NADP

Experimental info

Mutagenesis

360

1

Y → F: Results in a 2.0-fold reduction in kcat for the diaphorase reaction. Ref.2

Mutagenesis

360

1

Y → G: Results in a 302-fold reduction in kcat for the diaphorase reaction. Ref.2

Mutagenesis

360

1

Y → S: Results in a 22-fold reduction in kcat for the diaphorase reaction. Ref.2

Mutagenesis

360

1

Y → W: Results in a 2.2-fold reduction in kcat for the diaphorase reaction. Ref.2

Secondary structure

1

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360

Helix Strand Turn

Details...

Beta strand

67 – 69

3

Beta strand

84 – 93

10

Beta strand

99 – 101

3

Beta strand

103 – 109

7

Beta strand

121 – 125

5

Beta strand

127 – 129

3

Beta strand

139 – 143

5

Beta strand

152 – 154

3

Beta strand

156 – 162

7

Beta strand

165 – 167

3

Beta strand

173 – 175

3

Helix

177 – 184

8

Beta strand

190 – 197

8

Beta strand

210 – 216

7

Helix

217 – 220

4

Helix

221 – 231

11

Beta strand

242 – 252

11

Helix

253 – 255

3

Helix

259 – 268

10

Turn

270 – 272

3

Beta strand

273 – 279

7

Turn

280 – 282

3

Helix

293 – 297

5

Helix

298 – 300

3

Helix

301 – 309

9

Beta strand

313 – 320

8

Helix

323 – 337

15

Helix

342 – 351

10

Beta strand

355 – 359

5

Sequences

	Sequence		Length	Mass (Da)
	P10933 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 7F1CC10DEBBA7B24	FASTA	360	40,194
	10 20 30 40 50 60 MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNN VSISGRVGTI RAQVTTEAPA 70 80 90 100 110 120 KVVKHSKKQD ENIVVNKFKP KEPYVGRCLL NTKITGDDAP GETWHMVFST EGEVPYREGQ 130 140 150 160 170 180 SIGIVPDGID KNGKPHKLRL YSIASSAIGD FGDSKTVSLC VKRLVYTNDA GEVVKGVCSN 190 200 210 220 230 240 FLCDLKPGSE VKITGPVGKE MLMPKDPNAT VIMLGTGTGI APFRSFLWKM FFEKHEDYQF 250 260 270 280 290 300 NGLAWLFLGV PTSSSLLYKE EFEKMKEKAP ENFRLDFAVS REQVNDKGEK MYIQTRMAQY 310 320 330 340 350 360 AEELWELLKK DNTFVYMCGL KGMEKGIDDI MVSLAAKDGI DWIEYKRTLK KAEQWNVEVY

References

[1]	"Characterisation of a full-length cDNA clone for pea ferredoxin-NADP+ reductase." Newman B.J., Gray J.C. Plant Mol. Biol. 10:511-520(1988) [Agricola: IND92000035] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Little Marvel. Tissue: Leaf.
[2]	"Probing the role of the carboxyl-terminal region of ferredoxin-NADP+ reductase by site-directed mutagenesis and deletion analysis." Orellano E.G., Calcaterra N.B., Carrillo N., Ceccarelli E.A. J. Biol. Chem. 268:19267-19273(1993) [PubMed: 8366077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 270-360, MUTAGENESIS OF TYR-360.
[3]	"Protein import into chloroplasts involves redox-regulated proteins." Kuechler M., Decker S., Hoermann F., Soll J., Heins L. EMBO J. 21:6136-6145(2002) [PubMed: 12426385] [Abstract] Cited for: INTERACTION WITH TIC62.
[4]	"A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies." Deng Z., Aliverti A., Zanetti G., Arakaki A.K., Ottado J., Orellano E.G., Calcaterra N.B., Ceccarelli E.A., Carrillo N., Karplus P.A. Nat. Struct. Biol. 6:847-853(1999) [PubMed: 10467097] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD AND NADP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12446 mRNA. Translation: CAA30978.1.
L15565 mRNA. Translation: AAB59349.1.
L15567 mRNA. Translation: AAB59303.1.
L15569 mRNA. Translation: AAB59304.1.

PIR

S04030.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QFY	X-ray	1.80	A/B	53-359	[»]
1QFZ	X-ray	1.70	A/B	53-359	[»]
1QG0	X-ray	2.50	A/B	53-360	[»]
1QGA	X-ray	2.00	A/B	53-359	[»]
2XNC	X-ray	2.90	A/B	51-360	[»]
3MHP	X-ray	1.70	A/B	66-360	[»]

ProteinModelPortal

P10933.

SMR

P10933. Positions 53-359.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10933. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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. FRD_Red. 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...

Entry information

Entry name

FENR1_PEA

Accession

Primary (citable) accession number: P10933

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program