FENR_BRASO
ID FENR_BRASO Reviewed; 342 AA.
AC A4YXZ8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=BRADO5079;
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=114615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278;
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(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; CU234118; CAL78774.1; -; Genomic_DNA.
DR RefSeq; WP_012028713.1; NC_009445.1.
DR AlphaFoldDB; A4YXZ8; -.
DR SMR; A4YXZ8; -.
DR STRING; 114615.BRADO5079; -.
DR EnsemblBacteria; CAL78774; CAL78774; BRADO5079.
DR KEGG; bra:BRADO5079; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_5; -.
DR OMA; PEKVIYD; -.
DR OrthoDB; 692968at2; -.
DR BioCyc; BSP114615:BRADO_RS23595-MON; -.
DR Proteomes; UP000001994; 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..342
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364811"
FT BINDING 17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ SEQUENCE 342 AA; 36983 MW; 907AB89552A52AF9 CRC64;
MSEAIKTDVL IIGAGPCGLF AVFELGLLDI KAHLIDILDK VGGQCAELYP EKPIYDIPGV
PMVTGQGLTD QLMEQIKPFS PTFHLGEMVS NVEKIGDPGF RVTTDAGKVF ECKVVVIAAG
GGSFQPKRPP VPGIEAYEGT SVFYAVRKME QFRGKNVVIV GGGDSALDWT LNLHPIAKRI
ALIHRRDDFR AAPHSVEQMR ALVASGKMDL RIGQVTALEG TNGQLSAATI KGNDNAVETI
PCEMMLPFFG LTMKLGPVAD WGIALEHNLI PVETSAFETS VPGIFAIGDI NTYPGKIKLI
LCGFHEGALM AQKAHRYVYP EKRLVFQYTT SSSSLQKKLG VN
