FENR_RHOP5
ID FENR_RHOP5 Reviewed; 342 AA.
AC Q07RK6;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=RPE_1478;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000463; ABJ05428.1; -; Genomic_DNA.
DR RefSeq; WP_011662914.1; NC_008435.1.
DR AlphaFoldDB; Q07RK6; -.
DR SMR; Q07RK6; -.
DR STRING; 316055.RPE_1478; -.
DR EnsemblBacteria; ABJ05428; ABJ05428; RPE_1478.
DR KEGG; rpe:RPE_1478; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_5; -.
DR OMA; PEKVIYD; -.
DR OrthoDB; 692968at2; -.
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.
FT CHAIN 1..342
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364914"
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; 37134 MW; 1A395E169B98A15C CRC64;
MSEAIKTDVL IVGAGPCGLF AVFELGLLDV KVHLVDILDK VGGQCAELYP EKPIYDIPGI
PMITGHGLTE SLMEQIKPFD PQFHLGEMIE TVEQIGDPGF RVTTDAGTVF ECKVLVVAAG
GGSFQPKRPP VPGVEHYEGK SVHYAVRKMD EFRGKDILIV GGGDSALDWT LNLNPICKSM
TLVHRRDDFR GAPHSVEQMR QLVASGKLDL KIGQITALQG ENGQLEGATI KLNDNSTAQI
KCDAMLPFFG LTMKLGPVAN WGLHLENNLI PVDTGTFETN VPGIFAIGDI NTYPGKLKLI
LSGFHEGALM AQKAVKYVYP DKRVVFQYTT SSTSLQKKLG VN
