FENR_CHLRE
ID FENR_CHLRE Reviewed; 354 AA.
AC P53991;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ferredoxin--NADP reductase, chloroplastic;
DE Short=FNR;
DE EC=1.18.1.2;
DE Flags: Precursor;
GN Name=PETH; Synonyms=FNR;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7846183; DOI=10.1104/pp.106.4.1715;
RA Kitayama M., Kitayama K., Togasaki R.K.;
RT "A cDNA clone encoding a ferredoxin-NADP+ reductase from Chlamydomonas
RT reinhardtii.";
RL Plant Physiol. 106:1715-1716(1994).
RN [2]
RP PROTEIN SEQUENCE OF 36-265, AND METHYLATION AT LYS-118; LYS-124 AND
RP LYS-170.
RA Decottignies P., Flesch V., Jacquot J.-P., Schmitter J.-M., le Marechal P.;
RT "Specific post-translational methylation of three lysine residues in
RT Chlamydomonas reinhardtii ferredoxin-NADP reductase.";
RL (In) Proceedings of XIth international conference on methods in protein
RL structure analysis, pp.45-45, Annecy (1996).
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 -!- PATHWAY: Energy metabolism; photosynthesis.
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 -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; U10545; AAA79131.1; -; mRNA.
DR PIR; T08035; T08035.
DR AlphaFoldDB; P53991; -.
DR SMR; P53991; -.
DR DIP; DIP-58595N; -.
DR IntAct; P53991; 1.
DR STRING; 3055.EDP00292; -.
DR PRIDE; P53991; -.
DR eggNOG; KOG1158; Eukaryota.
DR UniPathway; UPA00091; -.
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; 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; 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 Chloroplast; Direct protein sequencing; Electron transport; FAD;
KW Flavoprotein; Membrane; Methylation; NADP; Oxidoreductase; Photosynthesis;
KW Plastid; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 36..354
FT /note="Ferredoxin--NADP reductase, chloroplastic"
FT /id="PRO_0000019407"
FT DOMAIN 69..198
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 130..133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 151..153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 245..246
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 275..276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 313..314
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 118
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 124
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 170
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 354 AA; 39277 MW; 4927FBA0CF668FBD CRC64;
MASLRKPSNH ADRACSRRLR VATRVAGRRM CRPVAATKAS TAVTTDMSKR TVPTKLEEGE
MPLNTYSNKA PFKAKVRSVE KITGPKATGE TCHIIIETEG KIPFWEGQSY GVIPPGTKIN
SKGKEVPTAR LYSIASSRYG DDGDGQTASL CVRRAVYVDP ETGKEDPAKK GLCSNFLCDA
TPGTEISMTG PTGKVLLLPA DANAPLICVA TGTGIAPFRS FWRRCFIENV PSYKFTGLFW
LFMGVGNSDA KLYDEELQAI AKAYPGQFRL DYALSREQNN RKGGKMYIQD KVEEYADEIF
DLLDNGAHMY FCGLKGMMPG IQDMLERVAK EKGLNYEEWV EGLKHKNQWH VEVY
