RUTA_ECOD1
ID RUTA_ECOD1 Reviewed; 363 AA.
AC C9QZ64; E6P341;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=EcDH1_2630, ECDH1ME8569_0966;
OS Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIMB 12045 / K12 / DH1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=536056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33849 / DSM 4235 / NCIMB 12045 / K12 / DH1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Keasling J.D.;
RT "Complete sequence of Escherichia coli DH1.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33849 / DSM 4235 / NCIMB 12045 / K12 / DH1;
RX PubMed=21611185; DOI=10.1371/journal.pone.0019534;
RA Suzuki S., Ono N., Furusawa C., Ying B.W., Yomo T.;
RT "Comparison of sequence reads obtained from three next-generation
RT sequencing platforms.";
RL PLoS ONE 6:E19534-E19534(2011).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAJ42822.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001637; ACX40264.1; -; Genomic_DNA.
DR EMBL; AP012030; BAJ42822.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001340618.1; NC_017638.1.
DR AlphaFoldDB; C9QZ64; -.
DR SMR; C9QZ64; -.
DR KEGG; edh:EcDH1_2630; -.
DR KEGG; edj:ECDH1ME8569_0966; -.
DR PATRIC; fig|536056.19.peg.1023; -.
DR HOGENOM; CLU_027853_1_1_6; -.
DR OMA; ADYNFCF; -.
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_0000402594"
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; 39943 MW; 1A35F5DC9B7B8C54 CRC64;
MKIGVFVPIG NNGWLISTHA PQYMPTFELN KAIVQKAEHY HFDFALSMIK LRGFGGKTEF
WDHNLESFTL MAGLAAVTSR IQIYATAATL TLPPAIVARM AATIDSISGG RFGVNLVTGW
QKPEYEQMGI WPGDDYFSRR YDYLTEYVQV LRDLWGTGKS DFKGDFFTMN DCRVSPQPSV
PMKVICAGQS DAGMAFSARY ADFNFCFGKG VNTPTAFAPT AARMKQAAEQ TGRDVGSYVL
FMVIADETDD AARAKWEHYK AGADEEALSW LTEQSQKDTR SGTDTNVRQM ADPTSAVNIN
MGTLVGSYAS VARMLDEVAS VPGAEGVLLT FDDFLSGIET FGERIQPLMQ CRAHLPALTQ
EVA
