FENR_SHIFL
ID FENR_SHIFL Reviewed; 248 AA.
AC P28901;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 03-AUG-2022, entry version 141.
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; Synonyms=mvrA; OrderedLocusNames=SF4002, S3745;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=M4243;
RX PubMed=1400248; DOI=10.1128/jb.174.21.6981-6991.1992;
RA Truniger V., Boos W., Sweet G.;
RT "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella
RT flexneri.";
RL J. Bacteriol. 174:6981-6991(1992).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA77813.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN45435.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18765.1; -; Genomic_DNA.
DR EMBL; Z11766; CAA77813.1; ALT_FRAME; Genomic_DNA.
DR PIR; S23906; S23906.
DR RefSeq; NP_709728.1; NC_004337.2.
DR RefSeq; WP_000796320.1; NZ_WPGW01000012.1.
DR AlphaFoldDB; P28901; -.
DR SMR; P28901; -.
DR STRING; 198214.SF4002; -.
DR EnsemblBacteria; AAN45435; AAN45435; SF4002.
DR EnsemblBacteria; AAP18765; AAP18765; S3745.
DR GeneID; 1023471; -.
DR GeneID; 66672168; -.
DR KEGG; sfl:SF4002; -.
DR KEGG; sfx:S3745; -.
DR PATRIC; fig|198214.7.peg.4716; -.
DR HOGENOM; CLU_003827_3_0_6; -.
DR OMA; MTSEHYW; -.
DR OrthoDB; 707164at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..248
FT /note="Flavodoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000167644"
FT DOMAIN 2..101
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 50..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 74..76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 143..144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 173..174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 214..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 247..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P28861"
SQ SEQUENCE 248 AA; 27699 MW; 1D71D26F195EA512 CRC64;
MADWVTGKVT KVQNWTDALF SLTVHAPVLP FTAGQFTKLG LEIDGERVQR AYSYVNSPDN
PDLEFYLVTV PDGKLSPRLA ALKPGDEVQV VSEAAGFFVL DEVPDCETLW MLATGTAIGP
YLSILQLGKD LDRFKNLVLV HAARYAADLS YLPLMQELEK RYEGKLRIQT VVSRETAAGS
LTGRIPALIE SGELESAIGL PMNKETSHVM LCGNPQMVRD TQQLLKETRQ MTKHLRRRPG
HMTAEHYW
