ID   RUTF_ECO10              Reviewed;         164 AA.
AC   C8U5G9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=FMN reductase (NADH) RutF {ECO:0000255|HAMAP-Rule:MF_00833};
DE            EC=1.5.1.42 {ECO:0000255|HAMAP-Rule:MF_00833};
DE   AltName: Full=FMN reductase {ECO:0000255|HAMAP-Rule:MF_00833};
DE   AltName: Full=NADH-flavin reductase RutF {ECO:0000255|HAMAP-Rule:MF_00833};
DE   AltName: Full=NADH:flavin oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00833};
GN   Name=rutF {ECO:0000255|HAMAP-Rule:MF_00833}; OrderedLocusNames=ECO103_1053;
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC;
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T.,
RA   Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution of
RT   O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the reduction of FMN to FMNH2 which is used to
CC       reduce pyrimidine by RutA via the Rut pathway. {ECO:0000255|HAMAP-
CC       Rule:MF_00833}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.42;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00833};
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC       called GlnG) and repressed by RutR. {ECO:0000255|HAMAP-Rule:MF_00833}.
CC   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC       RutF subfamily. {ECO:0000255|HAMAP-Rule:MF_00833}.
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DR   EMBL; AP010958; BAI29898.1; -; Genomic_DNA.
DR   RefSeq; WP_001028095.1; NC_013353.1.
DR   AlphaFoldDB; C8U5G9; -.
DR   SMR; C8U5G9; -.
DR   EnsemblBacteria; BAI29898; BAI29898; ECO103_1053.
DR   GeneID; 66670715; -.
DR   KEGG; eoh:ECO103_1053; -.
DR   HOGENOM; CLU_059021_2_2_6; -.
DR   OMA; WFDRGYH; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:RHEA.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:InterPro.
DR   GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.110.10; -; 1.
DR   HAMAP; MF_00833; RutF; 1.
DR   InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR   InterPro; IPR019917; RutF.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   Pfam; PF01613; Flavin_Reduct; 1.
DR   SMART; SM00903; Flavin_Reduct; 1.
DR   TIGRFAMs; TIGR03615; RutF; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; NAD; Oxidoreductase.
FT   CHAIN           1..164
FT                   /note="FMN reductase (NADH) RutF"
FT                   /id="PRO_0000403008"
SQ   SEQUENCE   164 AA;  17747 MW;  786277D7EF22999A CRC64;
     MNIVDQQTFR DAMSCMGAAV NIITTDGPAG RAGFTASAVC SVTDTPPTLL VCLNRGASVW
     PVFNENRTLC VNTLSAGQEP LSNLFGGKTP MEHRFAAARW QTGVTGCPQL EEALVSFDCR
     ISQVVSVGTH DILFCAIEAI HRHATPYGLV WFDRSYHALM RPAC