ID   RUTA_ECOSM              Reviewed;         363 AA.
AC   B1LIZ3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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};
GN   OrderedLocusNames=EcSMS35_2113;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB15974.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1LIZ3; -.
DR   SMR; B1LIZ3; -.
DR   EnsemblBacteria; ACB15974; ACB15974; EcSMS35_2113.
DR   KEGG; ecm:EcSMS35_2113; -.
DR   HOGENOM; CLU_027853_1_1_6; -.
DR   OMA; ADYNFCF; -.
DR   Proteomes; UP000007011; 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_0000402602"
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;  39957 MW;  660CEC3E4051A829 CRC64;
     MKIGVFVPIG NNGWLISTHA PQYMPTFELN KAIVQKAEHY HFDFALSMIK LRGFGGKTEF
     WDHNLESFTL MAGLAAVTSR IQIYATAATL TLPPAIVARM AATIDSISGG RFGVNLVTGW
     QKPEYEQMGI WPGDDYFSRR YDYLTEYVQV LRDLWGSGKS DFKGDFFTMD DCRVSPQPSV
     PMKVICAGQS DAGMAFSARY ADFNFCFGKG VNTPTAFAPT AARMKQAAEQ TGRDVGSYVL
     FMVIADETDD AARAKWEHYK AGADEEALSW LTEQSQKDTR SGTDTNVRQM ADPTSAVNIN
     MGTLVGSYAS VARMLDEVAT VPGAEGVLLT FDDFLSGIEN FGERIQPLMQ CRAHLPALTQ
     EVA