FRE_ECOLI
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 03-AUG-2022, entry version 132.
DE RecName: Full=NAD(P)H-flavin reductase;
DE EC=1.5.1.41 {ECO:0000250|UniProtKB:Q9L6L9};
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=fadI, flrD, fsrC, ubiB; OrderedLocusNames=b3844, JW3820;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RX PubMed=2050627; DOI=10.1128/jb.173.12.3673-3679.1991;
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 coli
RT 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 gene
RT required for full activation of structural genes of the AD regulon in
RT 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 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 from
RT 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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP CHARACTERIZATION, AND SUBUNIT.
RC STRAIN=K12;
RX 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 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. {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:0000269|PubMed:1601132}.
CC -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC oxidoreductase family. {ECO:0000305}.
CC -!- CAUTION: Was originally assigned to be ubiB.
CC {ECO:0000305|PubMed:1379743}.
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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; NP_418286.1; NC_000913.3.
DR RefSeq; WP_000209826.1; NZ_STEB01000021.1.
DR PDB; 1QFJ; X-ray; 2.20 A; A/B/C/D=2-233.
DR PDBsum; 1QFJ; -.
DR AlphaFoldDB; P0AEN1; -.
DR SMR; P0AEN1; -.
DR BioGRID; 4262003; 14.
DR IntAct; P0AEN1; 14.
DR STRING; 511145.b3844; -.
DR jPOST; P0AEN1; -.
DR PaxDb; P0AEN1; -.
DR PRIDE; P0AEN1; -.
DR EnsemblBacteria; AAC76847; AAC76847; b3844.
DR EnsemblBacteria; BAE77459; BAE77459; BAE77459.
DR GeneID; 66672250; -.
DR GeneID; 948325; -.
DR KEGG; ecj:JW3820; -.
DR KEGG; eco:b3844; -.
DR PATRIC; fig|511145.12.peg.3958; -.
DR EchoBASE; EB0330; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_7_4_6; -.
DR InParanoid; P0AEN1; -.
DR OMA; PCRHEGE; -.
DR PhylomeDB; P0AEN1; -.
DR BioCyc; EcoCyc:FMNREDUCT-MON; -.
DR BioCyc; MetaCyc:FMNREDUCT-MON; -.
DR BRENDA; 1.5.1.41; 2026.
DR EvolutionaryTrace; P0AEN1; -.
DR PRO; PR:P0AEN1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008047; F:enzyme activator activity; IDA:EcoCyc.
DR GO; GO:0052875; F:riboflavin reductase (NADH) activity; IDA:EcoCyc.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:EcoCyc.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0030091; P:protein repair; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; FMN;
KW Ion transport; Iron; Iron transport; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2050627"
FT CHAIN 2..233
FT /note="NAD(P)H-flavin reductase"
FT /id="PRO_0000068144"
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"
FT STRAND 3..17
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:1QFJ"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1QFJ"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1QFJ"
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
