ID   RUTA_ECO44              Reviewed;         363 AA.
AC   D3H125;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Pyrimidine monooxygenase RutA {ECO:0000255|HAMAP-Rule:MF_01699};
DE            EC=1.14.99.46 {ECO:0000255|HAMAP-Rule:MF_01699};
GN   Name=rutA {ECO:0000255|HAMAP-Rule:MF_01699}; OrderedLocusNames=EC042_1087;
OS   Escherichia coli O44:H18 (strain 042 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=216592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=042 / EAEC;
RX   PubMed=20098708; DOI=10.1371/journal.pone.0008801;
RA   Chaudhuri R.R., Sebaihia M., Hobman J.L., Webber M.A., Leyton D.L.,
RA   Goldberg M.D., Cunningham A.F., Scott-Tucker A., Ferguson P.R.,
RA   Thomas C.M., Frankel G., Tang C.M., Dudley E.G., Roberts I.S., Rasko D.A.,
RA   Pallen M.J., Parkhill J., Nataro J.P., Thomson N.R., Henderson I.R.;
RT   "Complete genome sequence and comparative metabolic profiling of the
RT   prototypical enteroaggregative Escherichia coli strain 042.";
RL   PLoS ONE 5:E8801-E8801(2010).
CC   -!- FUNCTION: Catalyzes the pyrimidine ring opening between N-3 and C-4 by
CC       an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen
CC       atoms in the process to yield ureidoacrylate peracid, that immediately
CC       reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN-
CC       N(5)-oxide reacts spontaneously with NADH to produce FMN. Requires the
CC       flavin reductase RutF to regenerate FMN in vivo. {ECO:0000255|HAMAP-
CC       Rule:MF_01699}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NADH + O2 + uracil = (Z)-3-ureidoacrylate + FMN + H(+)
CC         + H2O + NAD(+); Xref=Rhea:RHEA:31587, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57618, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:59891; EC=1.14.99.46;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01699};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NADH + O2 + thymine = (Z)-2-methylureidoacrylate + FMN
CC         + H(+) + H2O + NAD(+); Xref=Rhea:RHEA:31599, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57618, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:143783; EC=1.14.99.46;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01699};
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC       called GlnG) and repressed by RutR. {ECO:0000255|HAMAP-Rule:MF_01699}.
CC   -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01699}.
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DR   EMBL; FN554766; CBG33909.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3H125; -.
DR   SMR; D3H125; -.
DR   KEGG; elo:EC042_1087; -.
DR   PATRIC; fig|216592.3.peg.1125; -.
DR   HOGENOM; CLU_027853_1_1_6; -.
DR   OMA; ADYNFCF; -.
DR   Proteomes; UP000001407; Chromosome.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0052614; F:uracil oxygenase activity; IEA:RHEA.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.30; -; 1.
DR   HAMAP; MF_01699; RutA; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR019914; Pyrimidine_monooxygenase_RutA.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR03612; RutA; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..363
FT                   /note="Pyrimidine monooxygenase RutA"
FT                   /id="PRO_0000402615"
FT   BINDING         49..50
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         115
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         124
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         140..141
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         190
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
SQ   SEQUENCE   363 AA;  39975 MW;  250AF635FFEB6336 CRC64;
     MKIGVFVPIG NNGWLISTHA PQYMPTFELN KAIVQKAEHY HFDFALSMIK LRGFGGKTEF
     WDHNLESFTL MAGLAAVTSR IQIYATAATL TLPPAIVARM AATIDSISGG RFGVNLVTGW
     QKPEYEQMGI WPGDDYFSRR YDYLTEYVQV LRDLWGTGKS DFKGDFFTMN DCRVSPQPSV
     PMKVICAGQS DAGMAFSAQY ADFNFCFGKG VNTPTAFAPT AARMKQAAEQ TGRDVGSYVL
     FMVIADETDD AARTKWEHYK AGADEEALSW LTEQSQKDTR SGTDTNVRQM ADPTSAVNIN
     MGTLVGSYAS VARMLDEVAS VPGAEGVLLT FDDFLSGIET FGERIQPLMQ CRAHLPTLTQ
     EVA