ID   FENR_PEDPA              Reviewed;         328 AA.
AC   Q03H60;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ferredoxin--NADP reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE            Short=FNR {ECO:0000255|HAMAP-Rule:MF_01685};
DE            Short=Fd-NADP(+) reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE            EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN   OrderedLocusNames=PEPE_0366;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01685};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01685};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01685};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01685}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01685}.
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DR   EMBL; CP000422; ABJ67462.1; -; Genomic_DNA.
DR   RefSeq; WP_011673037.1; NC_008525.1.
DR   AlphaFoldDB; Q03H60; -.
DR   SMR; Q03H60; -.
DR   STRING; 278197.PEPE_0366; -.
DR   EnsemblBacteria; ABJ67462; ABJ67462; PEPE_0366.
DR   GeneID; 33062222; -.
DR   KEGG; ppe:PEPE_0366; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_5_9; -.
DR   OMA; PEKVIYD; -.
DR   OrthoDB; 692968at2; -.
DR   Proteomes; UP000000773; Chromosome.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01685; FENR2; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="Ferredoxin--NADP reductase"
FT                   /id="PRO_0000364894"
FT   BINDING         34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         120
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         323
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ   SEQUENCE   328 AA;  36365 MW;  75B91754C7913F17 CRC64;
     MTEMYDITII GGGPAGLFAG FYAGMRTAKT QIIESLPQAG GQVAALYPEK MIYDVGGYAG
     IKAANLAKEL EKQTRLVGTE IRLNETVVDI QAQADFYHVK TNRNEYDTRA ILLATGNGAF
     NPRKLAVEGL DHLEDKKIYY HMPDVEHFEN QDILVAGGGD SAIDIALMLE PIAKSISLVH
     RRQQFRGMER NVQHLQESTV KVMTPYLING VREAVEGIDV DLKEIGTEAL KATHFDKLIV
     NYGFTSSNKI IKGWEIDLTQ EHRMFAVDSL MHTNMKNIYA IGDGVEYPGK LRLIATAFGE
     GPIAVNQIMN DLYPGKRGPV HSTSMFEK