ID   RUTA_METED              Reviewed;         364 AA.
AC   C7CM36;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=METDI2412;
OS   Methylorubrum extorquens (strain DSM 6343 / CIP 106787 / DM4)
OS   (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=661410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6343 / CIP 106787 / DM4;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(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   -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01699}.
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DR   EMBL; FP103042; CAX24018.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7CM36; -.
DR   SMR; C7CM36; -.
DR   EnsemblBacteria; CAX24018; CAX24018; METD_I2412.
DR   KEGG; mdi:METDI2412; -.
DR   HOGENOM; CLU_027853_1_1_5; -.
DR   OMA; ADYNFCF; -.
DR   Proteomes; UP000008070; 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..364
FT                   /note="Pyrimidine monooxygenase RutA"
FT                   /id="PRO_0000402630"
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   364 AA;  39856 MW;  09CFB358D62DA03F CRC64;
     MNIGVFIPIG NNGWLLSENA PQYMPSFELN KQITLKAEQH GLDFVLSMIK LRGFGGKTEF
     WDHNLESFTL MAGLAAVTSR IKLYATAPTL CLPPAIVARM ASTIDSISNG RFGLNLVTGW
     QRPEYAQMGL WPGDEYFGRR YEYLSEYAQV LRELWETGRS DLKGEFFQME DCRLSPRPQA
     EMKIICAGQS AAGMAFTATY ADYNFCFGKG VNTPTAFAPT VERLEEAKAK TGRDVSSYVL
     FMVISDETDE AARAKWEHYK AGADAEAIAW LGLQGAADTK SGADTNIRQM ADPTSAVNIN
     MGTLVGSHAT VAALLDEVVT VPGTGGVLLV FDDFLKGLDD FGTKIQPLMR SRRHVTGEAL
     AEVA