P41346 (FENR_VICFA) 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

Vicia faba (Broad bean) (Faba vulgaris)

Taxonomic identifier

3906 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Chloroplast Potential
	Chain	53 – 363	311	Ferredoxin--NADP reductase, chloroplastic		PRO_0000019410
Regions
	Domain	84 – 206	123	FAD-binding FR-type
	Nucleotide binding	142 – 145	4	FAD By similarity
	Nucleotide binding	163 – 165	3	FAD By similarity
	Nucleotide binding	180 – 182	3	FAD By similarity
	Nucleotide binding	253 – 254	2	NADP By similarity
	Nucleotide binding	283 – 284	2	NADP By similarity
	Nucleotide binding	322 – 323	2	NADP By similarity
Sites
	Binding site	145	1	NADP By similarity
	Binding site	165	1	NADP By similarity
	Binding site	169	1	FAD By similarity
	Binding site	221	1	FAD By similarity
	Binding site	221	1	NADP; via amide nitrogen By similarity
	Binding site	293	1	NADP By similarity
	Binding site	361	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P41346 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: CB0C8CC6D3203063	FASTA	363	40,579
	10 20 30 40 50 60 MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNS VSISGRVGTI RAQITTEAEA 70 80 90 100 110 120 PVTKVVKHSK KQDEGIVVNK FKPKEPYVGR CLLNTKITGD DAPGETWHMV FTTEGEVPYR 130 140 150 160 170 180 EGQSIGIVPD GIDKNGKPHK LRLYSIASSA IGDFGDSKTV SLCVKRLVYT NDAGEVVKGV 190 200 210 220 230 240 CSNFLCDLKP GSEVKITGPV GKEMLMPKDP NATVIMLGTG TGIAPFRSFL WKMFFEKHED 250 260 270 280 290 300 YKFNGLAWLF LGVPTSSSLL YKEEFEKMKE KAPENFRLDF AVSREQVNDK GEKMYIQTRM 310 320 330 340 350 360 AQYAEELWEL LKKDNTFVYM CGLKGMEKGI DDIMVSIRPK DGIDWIEYKR TLKKAEQWNV EVY

References

[1]	Lax A.R., Cary J.W. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14956 mRNA. Translation: AAA21758.1.
3D structure databases
ProteinModelPortal	P41346.
SMR	P41346. Positions 53-363.
ModBase	Search...
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

FENR_VICFA

Accession

Primary (citable) accession number: P41346

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program