FENR_BUCBP
ID FENR_BUCBP Reviewed; 249 AA.
AC Q89A28;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=bbp_527;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27229.1; -; Genomic_DNA.
DR RefSeq; WP_011091630.1; NC_004545.1.
DR AlphaFoldDB; Q89A28; -.
DR SMR; Q89A28; -.
DR STRING; 224915.bbp_527; -.
DR EnsemblBacteria; AAO27229; AAO27229; bbp_527.
DR GeneID; 56471061; -.
DR KEGG; bab:bbp_527; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_3_0_6; -.
DR OMA; MTSEHYW; -.
DR OrthoDB; 707164at2; -.
DR Proteomes; UP000000601; 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;
KW Reference proteome.
FT CHAIN 1..249
FT /note="Flavodoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000167642"
FT DOMAIN 2..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 51..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 75..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 144..145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 174..175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 215..217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 248..249
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
SQ SEQUENCE 249 AA; 29335 MW; 16E351770724413B CRC64;
MNTWITAKII KIKKWKNNLF SVIVNAPISP FTAGQFTKLG YQKKNGKIIQ RAYSFVNAPH
EKNLEFYMVL IKNGQLTTKL YNLNNTDHIQ IKKKSYGFFT LNEIPTCKIL WMFATGTGIG
PYLSMLKYQK NTEKFQKIVL IHAVRYRHDL TYFNEINNLK NIYNKKLYTQ FIISREKTNF
SLSGRIPQLL KTEELEKHIN LFIENNTSHV MLCGNPDMVK QTQNFLINNK NMKKHLRRKP
GQISSENYW
