ID   FENR_STRA5              Reviewed;         330 AA.
AC   Q8DYW9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=SAG1353;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009948; AAN00224.1; -; Genomic_DNA.
DR   RefSeq; NP_688351.1; NC_004116.1.
DR   RefSeq; WP_001044158.1; NC_004116.1.
DR   AlphaFoldDB; Q8DYW9; -.
DR   SMR; Q8DYW9; -.
DR   STRING; 208435.SAG1353; -.
DR   EnsemblBacteria; AAN00224; AAN00224; SAG1353.
DR   GeneID; 66886217; -.
DR   KEGG; sag:SAG1353; -.
DR   PATRIC; fig|208435.3.peg.1361; -.
DR   HOGENOM; CLU_031864_5_5_9; -.
DR   OMA; PEKVIYD; -.
DR   Proteomes; UP000000821; 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..330
FT                   /note="Ferredoxin--NADP reductase"
FT                   /id="PRO_0000364952"
FT   BINDING         35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         90
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         123
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         326
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ   SEQUENCE   330 AA;  36387 MW;  879B028823786140 CRC64;
     MNKTIYDITI VGGGPVGLFA AFYAGLRGVS VKIIESLSEL GGQPAILYPE KKIYDIPGYP
     VITGRELIDK HIEQLERFKD SIEICLKEEV LSFEKVDDVF TIQTDKDQHL SRAIVFACGN
     GAFAPRLLGL ENEENYADNN LFYNVTKLEQ FAGKHVVICG GGDSAVDWAN ELDKIAASVA
     IVHRRDAFRA HEHSVDILKA SGVRILTPYV PIGLNGDSQR VSSLVVQKVK GDEVIELPLD
     NLIVSFGFST SNKNLRYWNL DYKRSSINVS SLFETTQEGV YAIGDAANYP GKVELIATGY
     GEAPVAINQA INYIYPDRDN RVVHSTSLIK