RUTF_SHIFL
ID RUTF_SHIFL Reviewed; 152 AA.
AC Q83LK9; Q7UD00;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 4.
DT 25-MAY-2022, entry version 104.
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};
GN OrderedLocusNames=SF1010, S1080;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42636.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16521.1; -; Genomic_DNA.
DR RefSeq; NP_706929.2; NC_004337.2.
DR AlphaFoldDB; Q83LK9; -.
DR SMR; Q83LK9; -.
DR STRING; 198214.SF1010; -.
DR EnsemblBacteria; AAN42636; AAN42636; SF1010.
DR EnsemblBacteria; AAP16521; AAP16521; S1080.
DR GeneID; 1023968; -.
DR KEGG; sfl:SF1010; -.
DR KEGG; sfx:S1080; -.
DR PATRIC; fig|198214.7.peg.1174; -.
DR HOGENOM; CLU_059021_2_2_6; -.
DR OMA; WFDRGYH; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000403044"
SQ SEQUENCE 152 AA; 16358 MW; E976963101677A34 CRC64;
MSCMGAAVNI ITTDGPAGRA GFTASAVCSV TDTPPTLLVC LNRGASVWPV FNENRTLCVN
TLSAGQEPLS NLFGGKTPME HRFAAARWQT GVTGCPQLEE ALVSFDCRIS QVVSVGTHDI
LFCAIEAIHR HTTPYGLVWF DRSYHALMRP AC