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   16-JUN-2009, entry version 30.
DE   RecName: Full=NAD(P)H-flavin reductase;
DE            EC=1.5.1.29;
DE            EC=1.16.1.3;
DE   AltName: Full=FMN reductase;
DE   AltName: Full=NAD(P)H:flavin oxidoreductase;
DE   AltName: Full=Aquacobalamin reductase;
DE   AltName: Full=Ferrisiderophore reductase C;
GN   Name=fre; Synonyms=ubiB; OrderedLocusNames=c4791;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of 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. Seems to reduces the complexed Fe(3+) iron
CC       of siderophores to Fe(2+), thus releasing it from the chelator (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: FMNH(2) + NAD(P)(+) = FMN + NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: 2 cob(II)alamin + NAD(+) = 2
CC       aquacob(III)alamin + NADH.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the fre/luxG FAD/NAD(P) flavoprotein
CC       oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE014075; AAN83224.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_756650.2; -.
DR   SMR; P0AEN2; 2-233.
DR   GeneID; 1035669; -.
DR   GenomeReviews; AE014075_GR; c4791.
DR   KEGG; ecc:c4791; -.
DR   HOGENOM; P0AEN2; -.
DR   OMA; P0AEN2; ETTLYWG.
DR   BRENDA; 1.16.1.3; 292881.
DR   BRENDA; 1.5.1.29; 292881.
DR   GO; GO:0047138; F:aquacobalamin reductase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR008333; OxRdtase_FAD-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   InterPro; IPR001221; Phe_hydroxylase.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; FMN; Ion transport; Iron;
KW   Iron transport; NAD; NADP; Oxidoreductase; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    233       NAD(P)H-flavin reductase.
FT                                /FTId=PRO_0000068146.
FT   DOMAIN        2     99       FAD-binding FR-type.
FT   NP_BIND     111    115       Pyridine (By similarity).
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
//