FRE_ECO57
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 03-AUG-2022, entry version 100.
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=ubiB; OrderedLocusNames=Z5365, ECs4772;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
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 PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT 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. {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}.
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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_312799.1; NC_002695.1.
DR RefSeq; WP_000209826.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AEN3; -.
DR SMR; P0AEN3; -.
DR STRING; 155864.EDL933_5164; -.
DR EnsemblBacteria; AAG59038; AAG59038; Z5365.
DR EnsemblBacteria; BAB38195; BAB38195; ECs_4772.
DR GeneID; 66672250; -.
DR GeneID; 915131; -.
DR KEGG; ece:Z5365; -.
DR KEGG; ecs:ECs_4772; -.
DR PATRIC; fig|386585.9.peg.4981; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_7_4_6; -.
DR OMA; PCRHEGE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; 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_0000068145"
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
