ID   RUTA_METPB              Reviewed;         376 AA.
AC   B1ZB15;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Mpop_1075;
OS   Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS   (Methylobacterium populi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=441620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., 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., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001029; ACB79250.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1ZB15; -.
DR   SMR; B1ZB15; -.
DR   STRING; 441620.Mpop_1075; -.
DR   EnsemblBacteria; ACB79250; ACB79250; Mpop_1075.
DR   KEGG; mpo:Mpop_1075; -.
DR   eggNOG; COG2141; Bacteria.
DR   HOGENOM; CLU_027853_1_1_5; -.
DR   OMA; ADYNFCF; -.
DR   Proteomes; UP000007136; 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; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Pyrimidine monooxygenase RutA"
FT                   /id="PRO_0000402632"
FT   BINDING         61..62
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         127
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         136
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         152..153
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         202
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
SQ   SEQUENCE   376 AA;  41046 MW;  2A310D30EF72F664 CRC64;
     MTQANNHANN HAMNIGVFIP IGNNGWLLSE NAPQYMPSFE LNKQITLKAE QYGLDFALSM
     IKLRGFGGKT EFWDHNLESF TLMAGLAAVT SRIKLYATAP TLCLPPAIVA RMASTIDSIS
     NGRFGLNLVT GWQRPEYSQM GLWPGDEYFG RRYAYLSEYA QVLRDLWETG SSDLKGEFFQ
     MEDCRLSPRP QAEMKIICAG QSAAGMAFTA TYADYNFCFG KGVNTPTAFA PTVERLEEAK
     AKTGRDVSSY VLFMIISDET DEAARAKWEH YKAGADQEAI AWLGLQGAAD TKSGADTNIR
     QMADPTSAVN INMGTLVGSY ATVAALLDEV VTVPGTGGVL LVFDDFLKGL DDFGTKIQPL
     MASRRHVTGE ALAEVA