RUTF_SHIF2
ID RUTF_SHIF2 Reviewed; 164 AA.
AC D2AC38;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=SFxv_1096;
OS Shigella flexneri serotype X (strain 2002017).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=591020;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002017;
RX PubMed=19955273; DOI=10.1128/jcm.00614-09;
RA Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT clone of Shigella flexneri.";
RL J. Clin. Microbiol. 48:419-426(2010).
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; CP001383; ADA73356.1; -; Genomic_DNA.
DR RefSeq; WP_001028096.1; NC_017328.1.
DR AlphaFoldDB; D2AC38; -.
DR SMR; D2AC38; -.
DR EnsemblBacteria; ADA73356; ADA73356; SFxv_1096.
DR KEGG; sfe:SFxv_1096; -.
DR PATRIC; fig|591020.3.peg.1170; -.
DR HOGENOM; CLU_059021_2_2_6; -.
DR OMA; WFDRGYH; -.
DR Proteomes; UP000001884; 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.
FT CHAIN 1..164
FT /note="FMN reductase (NADH) RutF"
FT /id="PRO_0000403046"
SQ SEQUENCE 164 AA; 17777 MW; 786277D7F423299A CRC64;
MNIVDQQTFR DAMSCMGAAV NIITTDGPAG RAGFTASAVC SVTDTPPTLL VCLNRGASVW
PVFNENRTLC VNTLSAGQEP LSNLFGGKTP MEHRFAAARW QTGVTGCPQL EEALVSFDCR
ISQVVSVGTH DILFCAIEAI HRHTTPYGLV WFDRSYHALM RPAC
