P41343 (FENR_MESCR) 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
Synonyms:	FNRA

Organism

Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum)

Taxonomic identifier

3544 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Aizoaceae › Mesembryanthemum

Protein attributes

Sequence length	365 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 – ?		Chloroplast Potential
	Chain	? – 365		Ferredoxin--NADP reductase, chloroplastic		PRO_0000019408
Regions
	Domain	86 – 208	123	FAD-binding FR-type
	Nucleotide binding	144 – 147	4	FAD By similarity
	Nucleotide binding	165 – 167	3	FAD By similarity
	Nucleotide binding	182 – 184	3	FAD By similarity
	Nucleotide binding	255 – 256	2	NADP By similarity
	Nucleotide binding	285 – 286	2	NADP By similarity
	Nucleotide binding	324 – 325	2	NADP By similarity
Sites
	Binding site	147	1	NADP By similarity
	Binding site	167	1	NADP By similarity
	Binding site	171	1	FAD By similarity
	Binding site	223	1	FAD By similarity
	Binding site	223	1	NADP; via amide nitrogen By similarity
	Binding site	295	1	NADP By similarity
	Binding site	363	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P41343 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 02A10BFB66EC15FC	FASTA	365	41,063
	10 20 30 40 50 60 MAAAVTAAVS FPSTKSTPLS TRTSSVITHE KINFNKVPLY YRNVSVGGKV GTIRAVASDV 70 80 90 100 110 120 EAPVAKVEKH SKKMEEGVIV NKYKPKNPYT GRCLLNTKIT GDDAPGETWH MVFSHEGEIP 130 140 150 160 170 180 YREGQSVGVI PEGIDKNGKP HKLRLYSIAS RPLGDFGDSK TVSLCVKRLI YTNDNGEIVK 190 200 210 220 230 240 GVCSNFLCDL KPGSEVVLTG PVGKEMLMPK DPNATIIMLA TGTGIAPFRS FLWKMFFEKH 250 260 270 280 290 300 DDYKFNGLAW LFLGVPTSSS LLYKEEFEKM KEKAPENFRL DFAVSREQTN EKGEKMYIQT 310 320 330 340 350 360 RMAQYDRELW ELLKKDNTYV YMCGLKGMEK GIDDIMVSLA AEDGIDWFDY KKQLKKAEQW NVEVY

References

[1]	"Expression during salt stress and nucleotide sequence of cDNA for ferredoxin-NADP+ reductase from Mesembryanthemum crystallinum." Michalowski C.B., Schmitt J.M., Bohnert H.J. Plant Physiol. 89:817-822(1989) [PubMed: 16666627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M25528 mRNA. Translation: AAA33029.1.
PIR	A44974.
3D structure databases
ProteinModelPortal	P41343.
SMR	P41343. Positions 65-365.
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_MESCR

Accession

Primary (citable) accession number: P41343

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program