ID E6WD94_PANSA Unreviewed; 363 AA.
AC E6WD94;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Pyrimidine monooxygenase RutA {ECO:0000256|HAMAP-Rule:MF_01699};
DE EC=1.14.99.46 {ECO:0000256|HAMAP-Rule:MF_01699};
GN Name=rutA {ECO:0000256|HAMAP-Rule:MF_01699};
GN OrderedLocusNames=Pat9b_1395 {ECO:0000313|EMBL:ADU68716.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU68716.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU68716.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU68716.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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:0000256|HAMAP-
CC 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:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01699};
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01699}.
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DR EMBL; CP002433; ADU68716.1; -; Genomic_DNA.
DR RefSeq; WP_013508577.1; NC_014837.1.
DR AlphaFoldDB; E6WD94; -.
DR STRING; 592316.Pat9b_1395; -.
DR KEGG; pao:Pat9b_1395; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_1_6; -.
DR OrthoDB; 9814695at2; -.
DR Proteomes; UP000001624; 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 CDD; cd01094; Alkanesulfonate_monoxygenase; 1.
DR Gene3D; 3.20.20.30; Luciferase-like domain; 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 NCBIfam; TIGR03612; RutA; 1.
DR PANTHER; PTHR42847; ALKANESULFONATE MONOOXYGENASE; 1.
DR PANTHER; PTHR42847:SF4; ALKANESULFONATE MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01699};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01699};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_01699};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01699};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01699}.
FT DOMAIN 1..319
FT /note="Luciferase-like"
FT /evidence="ECO:0000259|Pfam:PF00296"
FT BINDING 49..50
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01699"
FT BINDING 115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01699"
FT BINDING 124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01699"
FT BINDING 140..141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01699"
FT BINDING 190
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01699"
SQ SEQUENCE 363 AA; 40037 MW; 7AE1C7400869DE0B CRC64;
MKIGVFIPIG NNGWLISTHA PQYKPTFELN KAIVQKAEHY HFDFALSMIK LRGFGGKTEF
WDHNLESFTL MAGLAAVTSR IEIYATAATL TLPPAIVARM ASTIDSISNG RFGVNLVTGW
QKPEYEQMGL WPGDDYFASR YQYLTEYVTV LRDLWGSGQS DFKGEFFTMN DCRLSPQPQK
PMKVICAGQS DAGMAFSAQH ADYNFCFGKG VNTPTAFAPT ATRMKQAADK AGREVGSYVL
FMIIAAESDE AARAKWEHYK AGADEEALAW LTTQSQQDTK SGSDTNVRQM ADPTSAVNIN
MGTLVGSYAN VARMLDDVAG VEGTQGVLLT FDDFLQGIEE FGQFIQPLMQ CRHALIESQK
EVA
//
