FENR_SPIOL
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 03-AUG-2022, entry version 141.
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}.
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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 PRIDE; P00455; -.
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 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 Gene3D; 3.40.50.80; -; 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; PTHR43314; 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; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 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 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
