ID   FRE_ECO57               Reviewed;         233 AA.
AC   P0AEN3; P23486; P76768;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 27.
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=Z5365, ECs4772;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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.
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DR   EMBL; AE005174; AAG59038.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38195.1; -; Genomic_DNA.
DR   PIR; B86072; B86072.
DR   PIR; D91225; D91225.
DR   RefSeq; NP_290474.1; -.
DR   RefSeq; NP_312799.1; -.
DR   SMR; P0AEN3; 2-233.
DR   GeneID; 915131; -.
DR   GeneID; 960316; -.
DR   GenomeReviews; AE005174_GR; Z5365.
DR   GenomeReviews; BA000007_GR; ECs4772.
DR   KEGG; ece:Z5365; -.
DR   KEGG; ecs:ECs4772; -.
DR   HOGENOM; P0AEN3; -.
DR   OMA; P0AEN3; ETTLYWG.
DR   BioCyc; ECOL83334:ECS4772-MON; -.
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_0000068145.
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
//