ID   RUTF1_METEP             Reviewed;         202 AA.
AC   A9W3H7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=FMN reductase (NADH) RutF 1 {ECO:0000255|HAMAP-Rule:MF_00833};
DE            EC=1.5.1.42 {ECO:0000255|HAMAP-Rule:MF_00833};
DE   AltName: Full=FMN reductase 1 {ECO:0000255|HAMAP-Rule:MF_00833};
DE   AltName: Full=NADH-flavin reductase RutF 1 {ECO:0000255|HAMAP-Rule:MF_00833};
DE   AltName: Full=NADH:flavin oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_00833};
GN   Name=rutF1 {ECO:0000255|HAMAP-Rule:MF_00833}; OrderedLocusNames=Mext_1734;
OS   Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC       RutF subfamily. {ECO:0000255|HAMAP-Rule:MF_00833}.
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DR   EMBL; CP000908; ABY30133.1; -; Genomic_DNA.
DR   RefSeq; WP_012253313.1; NC_010172.1.
DR   AlphaFoldDB; A9W3H7; -.
DR   SMR; A9W3H7; -.
DR   STRING; 419610.Mext_1734; -.
DR   EnsemblBacteria; ABY30133; ABY30133; Mext_1734.
DR   KEGG; mex:Mext_1734; -.
DR   eggNOG; COG1853; Bacteria.
DR   HOGENOM; CLU_059021_2_2_5; -.
DR   OMA; CINVLPA; -.
DR   BioCyc; MEXT419610:MEXT_RS08800-MON; -.
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..202
FT                   /note="FMN reductase (NADH) RutF 1"
FT                   /id="PRO_0000403035"
FT   REGION          168..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   202 AA;  20724 MW;  AC180635BFEA3C10 CRC64;
     MTDSESAAAV SVDAAAYREA MSRLASAVHL ITTDGPGGRA GFTASAVCSV SDAPPTLLVC
     INRASSAYAA LTQNGTLCVN TLGEGHETVA SLFGGRTPVD ERFAAGTWRR LRSGAPALAD
     ALVSFDCRIV GRHAVGSHDV LYCAVEAVAA SGEADALLYS ERRYRTLPRT PRSGSAPAEP
     ARAPRAVGAR PAEGPALALR SA