RUTA_CROTZ
ID RUTA_CROTZ Reviewed; 378 AA.
AC C9Y0S7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Ctu_15930;
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX PubMed=21037008; DOI=10.1128/jb.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(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 -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01699}.
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DR EMBL; FN543093; CBA29797.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y0S7; -.
DR SMR; C9Y0S7; -.
DR PRIDE; C9Y0S7; -.
DR EnsemblBacteria; CBA29797; CBA29797; CTU_15930.
DR KEGG; ctu:CTU_15930; -.
DR PATRIC; fig|693216.3.peg.1518; -.
DR HOGENOM; CLU_027853_1_1_6; -.
DR OMA; ADYNFCF; -.
DR Proteomes; UP000002069; 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..378
FT /note="Pyrimidine monooxygenase RutA"
FT /id="PRO_0000402589"
FT BINDING 65..66
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT BINDING 131
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT BINDING 140
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT BINDING 156..157
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT BINDING 206
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
SQ SEQUENCE 378 AA; 41790 MW; 18AE9A2082C59900 CRC64;
MQRHATVLLP AKERFVMKIG VFVPIGNNGW LISTHAPQYM PTFELNKAIV QKAEQQQFDF
ALSMIKLRGF GGKTEFWDHN LESFTLMAGL AAVTSRIQIY ATAATLTLPP AIVARMASTI
DSISGGRFGV NLVTGWQKPE YEQMGLWPGD EYFSRRYDYL TEYVHVLRDL WDTGQSDFKG
DYFTMNDCRV SPRPQQPMKV ICAGQSDAGM AFSAQHADYN FCFGKGVNTP AAFAPTAARM
KAAADKAGRN VGSYVLFMVI ADETDDAARA KWEHYKAGAD EEALSWLTEQ SQKDTRSGAD
TNVRQMADPT SAVNINMGTL VGSYASVARM LDEVAAVPGT EGVLLTFDDF LTGIDAFGEH
IQPLMRCRDH LRVTQEVA