ID FENR_SPIOL Reviewed; 369 AA. AC P00455; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 27-MAR-2024, entry version 146. DE RecName: Full=Ferredoxin--NADP reductase, chloroplastic; DE Short=FNR; DE EC=1.18.1.2; DE Flags: Precursor; GN Name=PETH; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2969782; DOI=10.1007/bf02427758; RA Jansen T., Reilaender H., Steppuhn J., Herrmann R.G.; RT "Analysis of cDNA clones encoding the entire precursor-polypeptide for RT ferredoxin:NADP+ oxidoreductase from spinach."; RL Curr. Genet. 13:517-522(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Alter J.M., Patrie W.J.; RT "Cloning and sequencing of the cDNA for precursor ferredoxin-NADP+: RT oxidoreductase from spinach."; RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 56-369. RX PubMed=6529571; DOI=10.1021/bi00321a046; RA Karplus P.A., Walsh K.A., Herriott J.R.; RT "Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase."; RL Biochemistry 23:6576-6583(1984). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120. RX PubMed=8455561; DOI=10.1007/bf00282808; RA Oelmueller R., Bolle C., Tyagi A.K., Niekrawietz N., Breit S.; RT "Characterization of the promoter from the single-copy gene encoding RT ferredoxin-NADP(+)-oxidoreductase from spinach."; RL Mol. Gen. Genet. 237:261-272(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND RP 2-PHOSPHO-AMP, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=1986412; DOI=10.1126/science.1986412; RA Karplus P.A., Daniels M.J., Herriott J.R.; RT "Atomic structure of ferredoxin-NADP+ reductase: prototype for a RT structurally novel flavoenzyme family."; RL Science 251:60-66(1991). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 74-369 OF MUTANTS ALA/GLN/LEU-367 RP IN COMPLEX WITH FAD, AND MUTAGENESIS OF GLU-367. RC TISSUE=Leaf; RX PubMed=9852055; DOI=10.1074/jbc.273.51.34008; RA Aliverti A., Deng Z., Ravasi D., Piubelli L., Karplus P.A., Zanetti G.; RT "Probing the function of the invariant glutamyl residue 312 in spinach RT ferredoxin-NADP+ reductase."; RL J. Biol. Chem. 273:34008-34015(1998). CC -!- FUNCTION: May play a key role in regulating the relative amounts of CC cyclic and non-cyclic electron flow to meet the demands of the plant CC for ATP and reducing power. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.18.1.2; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=35 uM for NADPH {ECO:0000269|PubMed:1986412}; CC -!- PATHWAY: Energy metabolism; photosynthesis. CC -!- INTERACTION: CC P00455; P00221: PETF; NbExp=3; IntAct=EBI-865079, EBI-864933; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast CC thylakoid membrane {ECO:0000305}; Peripheral membrane protein CC {ECO:0000305}; Stromal side {ECO:0000305}. Note=In the vicinity of the CC photosystem I in the non-stacked and fringe portion of the membrane. CC -!- MISCELLANEOUS: FNR is probably attached to the membrane by a specific CC binding protein. CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07981; CAA30791.1; -; mRNA. DR EMBL; M86349; AAA34029.1; -; mRNA. DR EMBL; X64351; CAA45703.1; -; Genomic_DNA. DR PIR; S00438; RDSPXX. DR PDB; 1BX0; X-ray; 1.90 A; A=56-369. DR PDB; 1BX1; X-ray; 1.90 A; A=56-369. DR PDB; 1FNB; X-ray; 1.70 A; A=56-369. DR PDB; 1FNC; X-ray; 2.00 A; A=56-369. DR PDB; 1FND; X-ray; 1.70 A; A=56-369. DR PDB; 1FRN; X-ray; 2.00 A; A=56-369. DR PDB; 1FRQ; X-ray; 1.95 A; A=56-369. DR PDBsum; 1BX0; -. DR PDBsum; 1BX1; -. DR PDBsum; 1FNB; -. DR PDBsum; 1FNC; -. DR PDBsum; 1FND; -. DR PDBsum; 1FRN; -. DR PDBsum; 1FRQ; -. DR AlphaFoldDB; P00455; -. DR SMR; P00455; -. DR IntAct; P00455; 2. DR KEGG; ag:CAA30791; -. DR BRENDA; 1.18.1.2; 5812. DR BRENDA; 1.19.1.1; 5812. DR SABIO-RK; P00455; -. DR UniPathway; UPA00091; -. DR EvolutionaryTrace; P00455; -. DR Proteomes; UP001155700; Unplaced. DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniPathway. DR CDD; cd06208; CYPOR_like_FNR; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR017927; FAD-bd_FR_type. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR015701; FNR. DR InterPro; IPR039261; FNR_nucleotide-bd. DR InterPro; IPR035442; FNR_plant_Cyanobacteria. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR PANTHER; PTHR43314; -; 1. DR PANTHER; PTHR43314:SF27; FERREDOXIN--NADP REDUCTASE, LEAF ISOZYME 2, CHLOROPLASTIC; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF501178; FNR-PetH; 1. DR PIRSF; PIRSF000361; Frd-NADP+_RD; 1. DR PRINTS; PR00371; FPNCR. DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Direct protein sequencing; Electron transport; KW FAD; Flavoprotein; Membrane; NADP; Oxidoreductase; Photosynthesis; Plastid; KW Reference proteome; Thylakoid; Transit peptide; Transport. FT TRANSIT 1..55 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:6529571" FT CHAIN 56..369 FT /note="Ferredoxin--NADP reductase, chloroplastic" FT /id="PRO_0000019412" FT DOMAIN 90..212 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716" FT BINDING 148..151 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1986412, FT ECO:0000269|PubMed:9852055" FT BINDING 151 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 169..171 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1986412, FT ECO:0000269|PubMed:9852055" FT BINDING 171 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT BINDING 175 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1986412, FT ECO:0000269|PubMed:9852055" FT BINDING 186..188 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1986412, FT ECO:0000269|PubMed:9852055" FT BINDING 227 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:1986412, FT ECO:0000269|PubMed:9852055" FT BINDING 227 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 259..260 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT BINDING 289..290 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT BINDING 299..301 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT BINDING 328..329 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 367 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT VARIANT 324 FT /note="F -> V" FT MUTAGEN 367 FT /note="E->A: Slightly reduced activity." FT /evidence="ECO:0000269|PubMed:9852055" FT MUTAGEN 367 FT /note="E->D,Q: Reduced activity." FT /evidence="ECO:0000269|PubMed:9852055" FT MUTAGEN 367 FT /note="E->L: Reduces activity by 99%." FT /evidence="ECO:0000269|PubMed:9852055" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 93..102 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 112..118 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 165..171 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 186..193 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 199..206 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 219..225 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 230..240 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 251..261 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 268..277 FT /evidence="ECO:0007829|PDB:1FNB" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 282..288 FT /evidence="ECO:0007829|PDB:1FNB" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 302..307 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 310..316 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 322..329 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 332..345 FT /evidence="ECO:0007829|PDB:1FNB" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:1FNB" FT HELIX 351..360 FT /evidence="ECO:0007829|PDB:1FNB" FT STRAND 364..369 FT /evidence="ECO:0007829|PDB:1FNB" SQ SEQUENCE 369 AA; 41188 MW; 1D0432BA47438A28 CRC64; MTTAVTAAVS FPSTKTTSLS ARSSSVISPD KISYKKVPLY YRNVSATGKM GPIRAQIASD VEAPPPAPAK VEKHSKKMEE GITVNKFKPK TPYVGRCLLN TKITGDDAPG ETWHMVFSHE GEIPYREGQS VGVIPDGEDK NGKPHKLRLY SIASSALGDF GDAKSVSLCV KRLIYTNDAG ETIKGVCSNF LCDLKPGAEV KLTGPVGKEM LMPKDPNATI IMLGTGTGIA PFRSFLWKMF FEKHDDYKFN GLAWLFLGVP TSSSLLYKEE FEKMKEKAPD NFRLDFAVSR EQTNEKGEKM YIQTRMAQYA VELWEMLKKD NTYFYMCGLK GMEKGIDDIM VSLAAAEGID WIEYKRQLKK AEQWNVEVY //