FENR_STRSV
ID FENR_STRSV Reviewed; 322 AA.
AC A3CM39;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SSA_0813;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44244.1; -; Genomic_DNA.
DR RefSeq; WP_011836730.1; NC_009009.1.
DR RefSeq; YP_001034794.1; NC_009009.1.
DR AlphaFoldDB; A3CM39; -.
DR SMR; A3CM39; -.
DR STRING; 388919.SSA_0813; -.
DR EnsemblBacteria; ABN44244; ABN44244; SSA_0813.
DR KEGG; ssa:SSA_0813; -.
DR PATRIC; fig|388919.9.peg.779; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_9; -.
DR OMA; PEKVIYD; -.
DR OrthoDB; 692968at2; -.
DR Proteomes; UP000002148; 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..322
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364973"
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 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ SEQUENCE 322 AA; 35155 MW; 895997CD2616D6EE CRC64;
MSELYDITIV GGGPVGLFAA FYAHLRQAKV KIIDSLPQLG GQPAILYPEK KILDVPGFTN
LSGEELTQRL IEQLETFQTE ICLNETVLDI VKSDDGFTIT TSQAQHQTKT IIIAMGGGAF
KPRALELDAA ESYSNLHYHV SNISQYAGKK VVVLGGGDSA VDWALAFEKI AETSLVHRRD
NFRALEHSVE ELKASSVEIK TPFVPSRLVG ENGKITHLEI SQVKGEESQL LPLDHLFVNY
GFKSSVGNLK DWGLELNRHK ILVNSKQETS VPGIYAAGDC CSYEGKIDLI ATGLGEAPTA
VNNAINHIYP DQKVQPKHST SL