RUTA_ACIAD
ID RUTA_ACIAD Reviewed; 369 AA.
AC Q6FFZ7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=ACIAD0027;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67010.1; -; Genomic_DNA.
DR RefSeq; WP_004930951.1; NC_005966.1.
DR AlphaFoldDB; Q6FFZ7; -.
DR SMR; Q6FFZ7; -.
DR STRING; 62977.ACIAD0027; -.
DR EnsemblBacteria; CAG67010; CAG67010; ACIAD0027.
DR GeneID; 45232561; -.
DR KEGG; aci:ACIAD0027; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_1_6; -.
DR OMA; ADYNFCF; -.
DR OrthoDB; 1434838at2; -.
DR BioCyc; ASP62977:ACIAD_RS00145-MON; -.
DR Proteomes; UP000000430; 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..369
FT /note="Pyrimidine monooxygenase RutA"
FT /id="PRO_0000402581"
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 369 AA; 40998 MW; AB64B310F3DD4844 CRC64;
MKIGVFCPIG NNGWLLSENA PQYMPSFELN KKIVQRAEHY GFDFALSMIK LRGFGGKTEF
WDHNLETFTL MAGLAAVTSK IKIYATAATL VMPPAIVARM ASTIDSISNG RFGLNVVTGW
QAPEYSQMGM WPGDEYFAKR YEYLSEYVQI LRELWATGQS DFKGEHFQME DCRVSPQPQA
EMKIICAGQS DTGLEFSAQH ADYNFVFGKG LNTPTAYAGI NDRLKHFTDQ TGRDVQTYVL
FMVIAAETDA EAMAKWQSYN DGADVEAINW LMNQGGKDTK SGADTNIRQM ASSVSPVNIN
MGTLVGSYEK VAAMLDEIAE IKGTEGILLT FDDFVQGVED FGERIQPLMT SRQDIVAEYQ
PVTPLEKSA