ID   FENR_SPISP              Reviewed;         294 AA.
AC   P00454;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ferredoxin--NADP reductase;
DE            Short=FNR;
DE            EC=1.18.1.2;
GN   Name=petH;
OS   Spirulina sp.
OC   Bacteria; Cyanobacteria; Spirulinales; Spirulinaceae; Spirulina.
OX   NCBI_TaxID=1157;
RN   [1]
RP   PROTEIN SEQUENCE, AND SEQUENCE REVISION.
RX   PubMed=6430889; DOI=10.1093/oxfordjournals.jbchem.a134759;
RA   Yao Y., Tamura T., Wada K., Matsubara H., Kodo K.;
RT   "Spirulina ferredoxin-NADP+ reductase. The complete amino acid sequence.";
RL   J. Biochem. 95:1513-1516(1984).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10.
RX   PubMed=6415047; DOI=10.1093/oxfordjournals.jbchem.a134367;
RA   Wada K., Tamura T., Matsubara H., Kodo K.;
RT   "Spirulina ferredoxin-NADP+ reductase. Further characterization with an
RT   improved preparation.";
RL   J. Biochem. 94:387-393(1983).
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   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Note=May be bound to the thylakoid membrane
CC       or anchored to the thylakoid-bound phycobilisomes.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000305}.
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DR   PIR; A00531; RDSGXX.
DR   AlphaFoldDB; P00454; -.
DR   SMR; P00454; -.
DR   PRIDE; P00454; -.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
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   Antenna complex; Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW   NADP; Oxidoreductase; Phycobilisome; Thylakoid.
FT   CHAIN           1..294
FT                   /note="Ferredoxin--NADP reductase"
FT                   /id="PRO_0000167635"
FT   DOMAIN          13..137
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         72..75
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..95
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         111..113
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..185
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         224..228
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         253..254
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  33349 MW;  8761AB97B04C8CD5 CRC64;
     AKTDIPVNIY KPKNPYIGKC LSNEELVREG GTGTVRHLIF DISGGDLRYL EGQSIGIIPP
     GTDNNGKPHK LRLYSIASTR HGDHVDDKTV SLCVRQLEYK HPETGETVYG VCSTYLCNLE
     AGADVAITGP VGKEMLLPED EDATIIMMAT GTGIAPFRAF LWRIFKEQHE DYKFKGLAWL
     FFGIPYSPNI LYQQELEELQ EEFPENFRLT LAISREQQNP EGGKMYIQDR IKENADQLWE
     LIQKPNTHTY ICGLKGMEGG IDEGMSAAAG KFDVDWSDYQ KELKKKHRWH VETY