ID   RUTF_PSEU5              Reviewed;         174 AA.
AC   A4VQH9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=PST_3602;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP81230.1; -; Genomic_DNA.
DR   RefSeq; WP_011914624.1; NC_009434.1.
DR   AlphaFoldDB; A4VQH9; -.
DR   SMR; A4VQH9; -.
DR   STRING; 379731.PST_3602; -.
DR   EnsemblBacteria; ABP81230; ABP81230; PST_3602.
DR   KEGG; psa:PST_3602; -.
DR   eggNOG; COG1853; Bacteria.
DR   HOGENOM; CLU_059021_2_2_6; -.
DR   OMA; WFDRGYH; -.
DR   Proteomes; UP000000233; Chromosome.
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; Reference proteome.
FT   CHAIN           1..174
FT                   /note="FMN reductase (NADH) RutF"
FT                   /id="PRO_0000403039"
SQ   SEQUENCE   174 AA;  18366 MW;  9CF0A05CCB01E11F CRC64;
     MQLAQCETTS QFSAPVIRED YRDAMARLAA AVNIITTDGP SGRAGFTATA VCSVTDEPPT
     LLVCLNRSAS AHPIVTANGQ LCVNTLAGAQ RDLSNLFGGK TPMAERFAAA QWSTGVTGSP
     LLDGATVSFD CRISHSASVG THDILYCEVL AVYRRDSSDA LVYFGRNYHG LSSS