FENR_BUCAI
ID FENR_BUCAI Reviewed; 252 AA.
AC P57641;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=BU581;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB13270.1; -; Genomic_DNA.
DR RefSeq; NP_240384.1; NC_002528.1.
DR RefSeq; WP_009874531.1; NC_002528.1.
DR AlphaFoldDB; P57641; -.
DR SMR; P57641; -.
DR STRING; 107806.10039236; -.
DR EnsemblBacteria; BAB13270; BAB13270; BAB13270.
DR KEGG; buc:BU581; -.
DR PATRIC; fig|107806.10.peg.586; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_3_0_6; -.
DR OMA; MTSEHYW; -.
DR Proteomes; UP000001806; 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; 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; 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..252
FT /note="Flavodoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000167640"
FT DOMAIN 2..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 54..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 78..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 147..148
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 177..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 218..220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 251..252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
SQ SEQUENCE 252 AA; 29537 MW; E161A47BBB9BD23B CRC64;
MNPWINADVL MVKKWTKNLF SLILNAPIEP FFAGQFNKLA LYNSNPLNKN KIQRAYSYVN
APSEKNLEIY IVRVLNGQLS NLLYNLHSGD KIFIKKKSFG FFIIDEIPDC EILWMFATGT
GIGPYCSILQ EGKNINRFNH IILTHAVRYQ NELTYLPLMK ELRQKYNGKL QIQTITSREK
HKNSLNGRIP FLLRNKILEK HVGFSINPQT SHVMLCGNPF MVKDTFLFLK NNRNMEKHLR
RKKGHITMEN YW
