RUTA_AGRFC
ID RUTA_AGRFC Reviewed; 363 AA.
AC P58759;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Pyrimidine monooxygenase RutA;
DE EC=1.14.99.46 {ECO:0000250|UniProtKB:P75898};
GN Name=rutA; OrderedLocusNames=Atu2500; ORFNames=AGR_C_4543;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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.
CC {ECO:0000250|UniProtKB:P75898}.
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 -!- 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 -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE007869; AAK88232.1; -; Genomic_DNA.
DR PIR; AI2883; AI2883.
DR PIR; G97659; G97659.
DR RefSeq; NP_355447.1; NC_003062.2.
DR RefSeq; WP_006312122.1; NC_003062.2.
DR AlphaFoldDB; P58759; -.
DR SMR; P58759; -.
DR STRING; 176299.Atu2500; -.
DR EnsemblBacteria; AAK88232; AAK88232; Atu2500.
DR GeneID; 66222695; -.
DR KEGG; atu:Atu2500; -.
DR PATRIC; fig|176299.10.peg.2512; -.
DR eggNOG; COG2141; Bacteria.
DR HOGENOM; CLU_027853_1_1_5; -.
DR OMA; ADYNFCF; -.
DR PhylomeDB; P58759; -.
DR Proteomes; UP000000813; Chromosome circular.
DR GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
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_0000197035"
FT BINDING 49..50
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255"
FT BINDING 124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255"
FT BINDING 140..141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255"
FT BINDING 190
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255"
SQ SEQUENCE 363 AA; 39840 MW; 4F2DF9068388D246 CRC64;
MEVGVFIPIG NNGWLLSENA PQYKPSFDLN KAITLKAEQY GFDFALSMIK LRGFGGKTEF
WDYNLESFTL MAGLAAVTSK IKLFGTAATL VMPPAIVARM ATTIDSISGG RFGINLITGW
QRPEYSQMGL WPGDDYFGDR YEYLGEYTSV LKELLTEGQS DFKGKFFQMD DCRMKPVPQG
DVKLICAGSS NSGMAFSAKF ADYSFCFGVG VNTPKAFAPT NERLLAATEK SGREVKSVVL
TMVLAEEKSE DAWAKWEHYK AGADEDAIKW LGLQSAVDTK SGSDTNVRHM SNPVSAVNIN
MGTLIGSYEE VAAMLDEMSE VPGTGGVMLT FDDFLEGVEK FGKYVQPLMK SRQHVLAELE
AAE