ID   FRE_ECOL6               Reviewed;         233 AA.
AC   P0AEN2; P23486; P76768;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=NAD(P)H-flavin reductase;
DE            EC=1.5.1.41 {ECO:0000250|UniProtKB:Q9L6L9};
DE   AltName: Full=Aquacobalamin reductase;
DE   AltName: Full=FMN reductase;
DE   AltName: Full=Ferrisiderophore reductase C;
DE   AltName: Full=NAD(P)H:flavin oxidoreductase;
DE   AltName: Full=Riboflavin reductase [NAD(P)H];
GN   Name=fre; Synonyms=ubiB; OrderedLocusNames=c4791;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reduction of soluble flavins by reduced
CC       pyridine nucleotides. {ECO:0000250|UniProtKB:Q9L6L9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin;
CC         Xref=Rhea:RHEA:19377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17607,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57986, ChEBI:CHEBI:58349; EC=1.5.1.41;
CC         Evidence={ECO:0000250|UniProtKB:Q9L6L9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + reduced riboflavin = 2 H(+) + NADH + riboflavin;
CC         Xref=Rhea:RHEA:31455, ChEBI:CHEBI:15378, ChEBI:CHEBI:17607,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57986; EC=1.5.1.41;
CC         Evidence={ECO:0000250|UniProtKB:Q9L6L9};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0AEN1}.
CC   -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83224.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN83224.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000209826.1; NC_004431.1.
DR   AlphaFoldDB; P0AEN2; -.
DR   SMR; P0AEN2; -.
DR   STRING; 199310.c4791; -.
DR   EnsemblBacteria; AAN83224; AAN83224; c4791.
DR   GeneID; 66672250; -.
DR   KEGG; ecc:c4791; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_7_4_6; -.
DR   OMA; PCRHEGE; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0052875; F:riboflavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
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   FAD; Flavoprotein; FMN; Ion transport; Iron; Iron transport; NAD; NADP;
KW   Oxidoreductase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..233
FT                   /note="NAD(P)H-flavin reductase"
FT                   /id="PRO_0000068146"
FT   DOMAIN          2..99
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   BINDING         111..115
FT                   /ligand="pyridine"
FT                   /ligand_id="ChEBI:CHEBI:16227"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  26242 MW;  0E64DE5A8FA0F12D CRC64;
     MTTLSCKVTS VEAITDTVYR VRIVPDAAFS FRAGQYLMVV MDERDKRPFS MASTPDEKGF
     IELHIGASEI NLYAKAVMDR ILKDHQIVVD IPHGEAWLRD DEERPMILIA GGTGFSYARS
     ILLTALARNP NRDITIYWGG REEQHLYDLC ELEALSLKHP GLQVVPVVEQ PEAGWRGRTG
     TVLTAVLQDH GTLAEHDIYI AGRFEMAKIA RDLFCSERNA REDRLFGDAF AFI