ID FRE_ECOLI Reviewed; 233 AA. AC P0AEN1; P23486; P76768; Q2M8E7; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 16-JUN-2009, entry version 36. 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=fadI, flrD, fsrC, ubiB; GN OrderedLocusNames=b3844, JW3820; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21. RX MEDLINE=91267929; PubMed=2050627; RA Spyrou G., Haggaard-Ljungquist E., Krook M., Joernvall H., Nilsson E., RA Reichard P.; RT "Characterization of the flavin reductase gene (fre) of Escherichia RT coli and construction of a plasmid for overproduction of the enzyme."; RL J. Bacteriol. 173:3673-3679(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RA Dirusso C.C., Shea O.; RT "FadI: identification, characterization, and nucleotide sequence of a RT gene required for full activation of structural genes of the AD RT regulon in Escherichia coli."; RL Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RA Saviranta P.J.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=92358234; PubMed=1379743; DOI=10.1126/science.1379743; RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.; RT "Analysis of the Escherichia coli genome: DNA sequence of the region RT from 84.5 to 86.5 minutes."; RL Science 257:771-778(1992). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP CHARACTERIZATION. RC STRAIN=K12; RX MEDLINE=92290008; PubMed=1601132; DOI=10.1016/0014-5793(92)80452-M; RA Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M., RA Guest J.R.; RT "The haemoglobin-like protein (HMP) of Escherichia coli has RT ferrisiderophore reductase activity and its C-terminal domain shares RT homology with ferredoxin NADP+ reductases."; RL FEBS Lett. 302:247-252(1992). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=99282168; PubMed=10353815; DOI=10.1021/bi982849m; RA Ingelman M., Ramaswamy S., Niviere V., Fontecave M., Eklund H.; RT "Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia RT coli."; RL Biochemistry 38:7040-7049(1999). 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. 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. CC -!- SIMILARITY: Belongs to the fre/luxG FAD/NAD(P) flavoprotein CC oxidoreductase family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC -!- CAUTION: Was originally (PubMed:1379743) assigned to be ubiB. 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; M61182; AAA23806.1; -; Genomic_DNA. DR EMBL; M85227; AAA23753.1; -; Genomic_DNA. DR EMBL; M74448; AAA91058.1; -; Genomic_DNA. DR EMBL; M87049; AAA67641.1; -; Genomic_DNA. DR EMBL; U00096; AAC76847.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77459.1; -; Genomic_DNA. DR PIR; A39434; A39434. DR RefSeq; AP_003958.1; -. DR RefSeq; NP_418286.1; -. DR PDB; 1QFJ; X-ray; 2.20 A; A/B/C/D=1-233. DR PDBsum; 1QFJ; -. DR GeneID; 948325; -. DR GenomeReviews; AP009048_GR; JW3820. DR GenomeReviews; U00096_GR; b3844. DR KEGG; ecj:JW3820; -. DR KEGG; eco:b3844; -. DR EchoBASE; EB0330; -. DR EcoGene; EG10334; fre. DR HOGENOM; P0AEN1; -. DR OMA; P0AEN1; ETTLYWG. DR BioCyc; EcoCyc:FMNREDUCT-MON; -. DR BioCyc; MetaCyc:FMNREDUCT-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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; FAD; KW Flavoprotein; FMN; Ion transport; Iron; Iron transport; NAD; NADP; KW Oxidoreductase; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 233 NAD(P)H-flavin reductase. FT /FTId=PRO_0000068144. FT DOMAIN 2 99 FAD-binding FR-type. FT NP_BIND 111 115 Pyridine (By similarity). FT STRAND 3 17 FT STRAND 19 27 FT STRAND 36 44 FT STRAND 46 50 FT STRAND 61 65 FT HELIX 75 84 FT STRAND 85 93 FT STRAND 102 104 FT STRAND 106 111 FT HELIX 115 128 FT STRAND 134 142 FT HELIX 143 145 FT HELIX 149 158 FT STRAND 162 170 FT STRAND 177 180 FT HELIX 182 189 FT STRAND 197 202 FT HELIX 204 217 FT HELIX 222 224 FT HELIX 229 232 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 //