RUTF_SHIDS
ID RUTF_SHIDS Reviewed; 152 AA.
AC Q32HQ4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=SDY_0982;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB61151.1; -; Genomic_DNA.
DR RefSeq; YP_402642.1; NC_007606.1.
DR AlphaFoldDB; Q32HQ4; -.
DR SMR; Q32HQ4; -.
DR STRING; 300267.SDY_0982; -.
DR EnsemblBacteria; ABB61151; ABB61151; SDY_0982.
DR KEGG; sdy:SDY_0982; -.
DR PATRIC; fig|300267.13.peg.1142; -.
DR HOGENOM; CLU_059021_2_2_6; -.
DR OMA; WFDRGYH; -.
DR Proteomes; UP000002716; 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..152
FT /note="FMN reductase (NADH) RutF"
FT /id="PRO_0000403043"
SQ SEQUENCE 152 AA; 16328 MW; E97696311A66CA34 CRC64;
MSCMGAAVNI ITTDGPAGRA GFTASAVCSV TDTPPTLLVC LNRGASVWPV FNENRTLCVN
TLSAGQEPLS NLFGGKTPME HRFAAARWQT GVTGCPQLEE ALVSFDCRIS QVVSVGTHDI
LFCAIEAIHR HATPYGLVWF DRSYHALMRP AC