RUTE_ECOL6
ID RUTE_ECOL6 Reviewed; 196 AA.
AC Q8FJ44;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable malonic semialdehyde reductase RutE {ECO:0000255|HAMAP-Rule:MF_01204};
DE EC=1.1.1.298 {ECO:0000255|HAMAP-Rule:MF_01204};
GN Name=rutE {ECO:0000255|HAMAP-Rule:MF_01204}; OrderedLocusNames=c1145;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: May reduce toxic product malonic semialdehyde to 3-
CC hydroxypropionic acid, which is excreted. {ECO:0000255|HAMAP-
CC Rule:MF_01204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoate + NADP(+) = 3-oxopropanoate + H(+) +
CC NADPH; Xref=Rhea:RHEA:26438, ChEBI:CHEBI:15378, ChEBI:CHEBI:16510,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.298; Evidence={ECO:0000255|HAMAP-Rule:MF_01204};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01204};
CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC called GlnG) and repressed by RutR. {ECO:0000255|HAMAP-Rule:MF_01204}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01204}.
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DR EMBL; AE014075; AAN79613.1; -; Genomic_DNA.
DR RefSeq; WP_001001177.1; NC_004431.1.
DR AlphaFoldDB; Q8FJ44; -.
DR SMR; Q8FJ44; -.
DR STRING; 199310.c1145; -.
DR EnsemblBacteria; AAN79613; AAN79613; c1145.
DR KEGG; ecc:c1145; -.
DR eggNOG; COG0778; Bacteria.
DR HOGENOM; CLU_084441_0_0_6; -.
DR OMA; LMVVNIG; -.
DR BioCyc; ECOL199310:C1145-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0035527; F:3-hydroxypropionate dehydrogenase (NADP+) 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 CDD; cd02148; RutE-like; 1.
DR Gene3D; 3.40.109.10; -; 1.
DR HAMAP; MF_01204; Oxidoreductase_RutE_HadB; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR InterPro; IPR023936; RutE-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; NAD; NADP; Oxidoreductase.
FT CHAIN 1..196
FT /note="Probable malonic semialdehyde reductase RutE"
FT /id="PRO_1000066138"
SQ SEQUENCE 196 AA; 21607 MW; 2D0FE1DA3B363368 CRC64;
MNEAVSPGAL STLFTDARTH NGWRETPVSD ETLREIYALM KWGPTSANCS PTRIVFIRTA
EGKERLRPAL SSGNLQKTLT APVTAIVAWD SEFYERLPQL FPHGDARSWF TSSPQLAEET
AFRNSSMQAA YLIVACRALG LDTGPMSGFD RQYVDDAFFA GSTLKSNLLI NIGYGDSSKL
FARLPRLSFE EACGLL