ID   C0ZCP3_BREBN            Unreviewed;       348 AA.
AC   C0ZCP3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 92.
DE   RecName: Full=Ferredoxin--NADP reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE            Short=FNR {ECO:0000256|HAMAP-Rule:MF_01685};
DE            Short=Fd-NADP(+) reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE            EC=1.18.1.2 {ECO:0000256|HAMAP-Rule:MF_01685};
GN   OrderedLocusNames=BBR47_25750 {ECO:0000313|EMBL:BAH43552.1};
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Paenibacillaceae;
OC   Brevibacillus.
OX   NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43552.1, ECO:0000313|Proteomes:UP000001877};
RN   [1] {ECO:0000313|EMBL:BAH43552.1, ECO:0000313|Proteomes:UP000001877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599
RC   {ECO:0000313|Proteomes:UP000001877};
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 reduced [2Fe-2S]-[ferredoxin] + NADP(+) + H(+) = 2 oxidized
CC         [2Fe-2S]-[ferredoxin] + NADPH; 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:0000256|HAMAP-
CC         Rule:MF_01685};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01685};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01685};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01685}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01685}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01685}.
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DR   EMBL; AP008955; BAH43552.1; -; Genomic_DNA.
DR   RefSeq; WP_012686256.1; NC_012491.1.
DR   AlphaFoldDB; C0ZCP3; -.
DR   STRING; 358681.BBR47_25750; -.
DR   KEGG; bbe:BBR47_25750; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_5_9; -.
DR   Proteomes; UP000001877; 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; FAD/NAD(P)-binding domain; 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   InterPro; IPR050097; Ferredoxin-NADP_redctase_2.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01685};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01685};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01685};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01685}; Reference proteome {ECO:0000313|Proteomes:UP000001877}.
FT   DOMAIN          8..302
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         287
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ   SEQUENCE   348 AA;  38439 MW;  BE0D27735A4B9C2A CRC64;
     MGEQLELFDV TIIGGGPAGM YAAFYSGMRD MKTKLIEAKE ELGGRMLIYP EKMIWDVGGV
     PPQLCEKLIA NLVQQAKTFD PTIVLGEAII GLEPQEDGTY ILVAKSGRRH WTRTIILALG
     RGILKMAKLE IEGAERYEVT NLHYTVQELE PFRGKHVLIS GGGDSAVDWA NELVQIAASV
     TVVHRRDVFG GHERNVKRMK ESSAIVRTPY AVTQLQSSDK ETIDKVTIRH LETDETEQIN
     VDAIIVNHGL KADFTGIKEW GLDMDEWNVF VSPRLATNLP GIFAAGDFAS FDSKITLIAG
     AFTDAAVAVN SAKLHIDPVA DRMAYVSSHN QRFKEKNKAL GVIDEDDE
//