ID RUTA_ECO10 Reviewed; 363 AA.
AC C8U5H4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=ECO103_1058;
OS Escherichia coli O103:H2 (strain 12009 / EHEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585395;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12009 / EHEC;
RX PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T.,
RA Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.;
RT "Comparative genomics reveal the mechanism of the parallel evolution of
RT O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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; AP010958; BAI29903.1; -; Genomic_DNA.
DR RefSeq; WP_001297176.1; NC_013353.1.
DR AlphaFoldDB; C8U5H4; -.
DR SMR; C8U5H4; -.
DR KEGG; eoh:ECO103_1058; -.
DR HOGENOM; CLU_027853_1_1_6; -.
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 CDD; cd01094; Alkanesulfonate_monoxygenase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 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 NCBIfam; TIGR03612; RutA; 1.
DR PANTHER; PTHR42847; ALKANESULFONATE MONOOXYGENASE; 1.
DR PANTHER; PTHR42847:SF4; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..363
FT /note="Pyrimidine monooxygenase RutA"
FT /id="PRO_0000402604"
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; 39915 MW; 250AF62F554A6E46 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 AARAKWEHYK AGADEEALSW LTEQSQKDTR SGTDTNVRQM ADPTSAVNIN
MGTLVGSYAS VARMLDEVAS VPGAEGVLLT FDDFLSGIET FGERIQPLMQ CRAHLPALTQ
EVA
//
