FENR_BUCAP
ID FENR_BUCAP Reviewed; 257 AA.
AC Q9Z615;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Flavodoxin/ferredoxin--NADP reductase {ECO:0000250|UniProtKB:P28861};
DE EC=1.18.1.2 {ECO:0000250|UniProtKB:P28861};
DE EC=1.19.1.1 {ECO:0000250|UniProtKB:P28861};
DE AltName: Full=Ferredoxin (flavodoxin):NADP(+) oxidoreductase {ECO:0000250|UniProtKB:P28861};
DE AltName: Full=Ferredoxin--NADP reductase {ECO:0000250|UniProtKB:P28861};
DE Short=FNR {ECO:0000250|UniProtKB:P28861};
DE AltName: Full=Flavodoxin--NADP reductase {ECO:0000250|UniProtKB:P28861};
DE Short=FLDR {ECO:0000250|UniProtKB:P28861};
GN Name=fpr; OrderedLocusNames=BUsg_560;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Clark M.A., Baumann P., Moran M.A.;
RT "Buchnera plasmid-associated trpEG probably originated from a chromosomal
RT location between hslU and fpr.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- FUNCTION: Transports electrons between flavodoxin or ferredoxin and
CC NADPH. {ECO:0000250|UniProtKB:P28861}.
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;
CC Evidence={ECO:0000250|UniProtKB:P28861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized
CC [flavodoxin]; Xref=Rhea:RHEA:50756, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:10623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.19.1.1;
CC Evidence={ECO:0000250|UniProtKB:P28861};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P28861};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28861}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF108665; AAD19635.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM68098.1; -; Genomic_DNA.
DR RefSeq; WP_011054064.1; NC_004061.1.
DR AlphaFoldDB; Q9Z615; -.
DR SMR; Q9Z615; -.
DR STRING; 198804.BUsg_560; -.
DR EnsemblBacteria; AAM68098; AAM68098; BUsg_560.
DR KEGG; bas:BUsg_560; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_3_0_6; -.
DR OMA; MTSEHYW; -.
DR OrthoDB; 707164at2; -.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd06195; FNR1; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR033892; FNR_bac.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..257
FT /note="Flavodoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000167641"
FT DOMAIN 2..110
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 59..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 83..85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 152..153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 182..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 223..225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 256..257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
SQ SEQUENCE 257 AA; 30079 MW; F1BF24F2D5FAA07B CRC64;
MNPWINANVL KVHKWTQNLF SLILNAEIAP FQAGQFTKLA LNEENINFSN NVKKKKIQRA
YSFVNAPSNK NLEIYIVRIL NGKLSNLLYN LKSGDNLFIK EKSFGFFTLD EIPNCKTLWM
FATGTGIGPY CSILQEYKNI NRFKNIILIH AVRYQNELTY LPLMKQLYKS YNGKLKIETI
VSREKNHNSL YGRIPLLLQN QILEKKIGLK INRNDSHVML CGNPAMVKDT YLFLQKDRCM
QKNLRRKHGH ITMENYW
