FENR1_CUPTR
ID FENR1_CUPTR Reviewed; 360 AA.
AC B3R4A7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ferredoxin--NADP reductase 1 {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=FNR 1 {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase 1 {ECO:0000255|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN OrderedLocusNames=RALTA_A1176;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69140.1; -; Genomic_DNA.
DR RefSeq; WP_012352468.1; NC_010528.1.
DR AlphaFoldDB; B3R4A7; -.
DR SMR; B3R4A7; -.
DR STRING; 977880.RALTA_A1176; -.
DR EnsemblBacteria; CAQ69140; CAQ69140; RALTA_A1176.
DR GeneID; 29760952; -.
DR KEGG; cti:RALTA_A1176; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_4; -.
DR OMA; LEQCAPF; -.
DR OrthoDB; 692968at2; -.
DR BioCyc; CTAI977880:RALTA_RS05620-MON; -.
DR Proteomes; UP000001692; Chromosome 1.
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..360
FT /note="Ferredoxin--NADP reductase 1"
FT /id="PRO_0000364825"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 141
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ SEQUENCE 360 AA; 38150 MW; 903CABEA8F247362 CRC64;
MPTATPATAP VTTTDVLIVG AGPVGLFAAF QAGVLGLKCE LIDVLDRAGG QCTELYPEKP
IYDIPAVPGC LAQDLVDRLL EQCAPFDFPM HFGQRAESVA EIPAPAASAG HAGHERLLVT
TDGGKRFDVA AVLICAGAGA FAPQRVSLPE AAALEGRHVH YAVRDVSHFA GKRVIVAGGG
DSALDWALAL RKVAARVTLL HRREGFRAAD GTVAEMRRAV AEGEMDFVVG MLGALRTEGA
DGGLSEVEVR TRDGSTVLPA EELVALYGLV SEPGPIAQWD LDMRAGRILV DTTTYESSRR
GIFAAGDIAF YPNKQKLILS GFHEAALALR KAYHYAFPEK ALVHVHTSNN AALKEKLTHA
