ID   RUTA_KLEP7              Reviewed;         363 AA.
AC   A6T7A2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=KPN78578_10120; ORFNames=KPN_01038;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR76473.1; -; Genomic_DNA.
DR   RefSeq; WP_004179293.1; NC_009648.1.
DR   AlphaFoldDB; A6T7A2; -.
DR   SMR; A6T7A2; -.
DR   STRING; 272620.KPN_01038; -.
DR   DNASU; 5340701; -.
DR   EnsemblBacteria; ABR76473; ABR76473; KPN_01038.
DR   KEGG; kpn:KPN_01038; -.
DR   HOGENOM; CLU_027853_1_1_6; -.
DR   OMA; ADYNFCF; -.
DR   Proteomes; UP000000265; 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..363
FT                   /note="Pyrimidine monooxygenase RutA"
FT                   /id="PRO_0000402626"
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;  39931 MW;  B05C4AC25538A5BD CRC64;
     MKIGVFVPIG NNGWLISTHA PQYMPTFELN KAIVQKAEHY HFDFALSMIK LRGFGGKTEF
     WDHNLESFTL MAGLAAVTSK IQIYATAATL TLPPAIVARM ASTIDSISGG RFGVNLVTGW
     QKPEYDQMGM WPGDDYFASR YDYLTEYVQV LRDLWGTGRS DFKGDYFTMN DCRVSPRPSQ
     PMKVICAGQS DAGMAFSAQH ADYNFCFGKG VNTPTAFAPT AARMMQAAEK TGRDVGSYVL
     FMVIADETDE AARAKWEHYK AGADEEALAW LTEQSQKDTR SGSDTNVRQM ADPTSAVNIN
     MGTLVGSYAS VARMLDEVAS VPGTDGVLLT FDDFLAGIDA FGERIQPLMR CRNHIASVTR
     EVA