ID   RUTF_SERP5              Reviewed;         175 AA.
AC   A8GCT2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Spro_1819;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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; CP000826; ABV40922.1; -; Genomic_DNA.
DR   RefSeq; WP_012006244.1; NC_009832.1.
DR   AlphaFoldDB; A8GCT2; -.
DR   SMR; A8GCT2; -.
DR   STRING; 399741.Spro_1819; -.
DR   EnsemblBacteria; ABV40922; ABV40922; Spro_1819.
DR   KEGG; spe:Spro_1819; -.
DR   eggNOG; COG1853; Bacteria.
DR   HOGENOM; CLU_059021_2_2_6; -.
DR   OMA; WFDRGYH; -.
DR   OrthoDB; 1681849at2; -.
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..175
FT                   /note="FMN reductase (NADH) RutF"
FT                   /id="PRO_0000403042"
SQ   SEQUENCE   175 AA;  18930 MW;  FAAA320C41CF0692 CRC64;
     MQSQTLLADT PLQSPYVEKQ DFRDAMARLG SAVNIITTDG PAGRAGFTAS AVCSVTDTPP
     TLLVCLNRSA SVYSVFKQNQ TLCVNTLAAE HESLSNLFGG KTPMELRFSA ARWSTLATGS
     PILHGAVVSF DCQIGQIVSV GTHDIFFCQA LALTRNDDSH GLAYFDRRYH SLLKQ