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   16-JUN-2009, entry version 64.
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.
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95148761; 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.,
RA   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
RL   protein structure analysis, pp.45-45, Annecy (1996).
CC   -!- FUNCTION: May play a key role in regulating the relative amounts
CC       of cyclic and non-cyclic electron flow to meet the demands of the
CC       plant for ATP and reducing power.
CC   -!- CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP(+) + H(+) = 2
CC       oxidized ferredoxin + NADPH.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Energy metabolism; photosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid,
CC       chloroplast thylakoid membrane; Peripheral membrane protein;
CC       Stromal side (Probable). Note=In the vicinity of the photosystem I
CC       in the non-stacked and fringe portion of the membrane.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1
CC       family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
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DR   EMBL; U10545; AAA79131.1; -; mRNA.
DR   PIR; T08035; T08035.
DR   HSSP; Q41736; 1JB9.
DR   PRIDE; P53991; -.
DR   BRENDA; 1.18.1.2; 144.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR012146; Frd-NADP+_RD.
DR   InterPro; IPR015701; FRD_Red.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   PANTHER; PTHR19384:SF1; FRD_Red; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000361; Frd-NADP+_RD; 1.
DR   PRINTS; PR00371; FPNCR.
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;
KW   Photosynthesis; Plastid; Thylakoid; Transit peptide; Transport.
FT   TRANSIT       1     35       Chloroplast.
FT   CHAIN        36    354       Ferredoxin--NADP reductase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000019407.
FT   DOMAIN       69    198       FAD-binding FR-type.
FT   NP_BIND     130    133       FAD (By similarity).
FT   NP_BIND     151    153       FAD (By similarity).
FT   NP_BIND     172    174       FAD (By similarity).
FT   NP_BIND     245    246       NADP (By similarity).
FT   NP_BIND     275    276       NADP (By similarity).
FT   NP_BIND     313    314       NADP (By similarity).
FT   BINDING     133    133       NADP (By similarity).
FT   BINDING     153    153       NADP (By similarity).
FT   BINDING     157    157       FAD (By similarity).
FT   BINDING     213    213       FAD (By similarity).
FT   BINDING     213    213       NADP; via amide nitrogen (By similarity).
FT   BINDING     285    285       NADP (By similarity).
FT   BINDING     352    352       NADP (By similarity).
FT   MOD_RES     118    118       N6,N6,N6-trimethyllysine.
FT   MOD_RES     124    124       N6,N6,N6-trimethyllysine.
FT   MOD_RES     170    170       N6,N6-dimethyllysine.
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
//