RUTB_ECOLI
ID RUTB_ECOLI Reviewed; 230 AA.
AC P75897;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ureidoacrylate amidohydrolase RutB;
DE EC=3.5.1.110 {ECO:0000269|PubMed:20400551};
GN Name=rutB; Synonyms=ycdL; OrderedLocusNames=b1011, JW5139;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION.
RX PubMed=11121068; DOI=10.1073/pnas.97.26.14674;
RA Zimmer D.P., Soupene E., Lee H.L., Wendisch V.F., Khodursky A.B.,
RA Peter B.J., Bender R.A., Kustu S.;
RT "Nitrogen regulatory protein C-controlled genes of Escherichia coli:
RT scavenging as a defense against nitrogen limitation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14674-14679(2000).
RN [5]
RP FUNCTION IN PYRIMIDINE CATABOLISM, AND NOMENCLATURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16540542; DOI=10.1073/pnas.0600521103;
RA Loh K.D., Gyaneshwar P., Markenscoff Papadimitriou E., Fong R., Kim K.-S.,
RA Parales R., Zhou Z., Inwood W., Kustu S.;
RT "A previously undescribed pathway for pyrimidine catabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5114-5119(2006).
RN [6]
RP INDUCTION.
RX PubMed=17919280; DOI=10.1111/j.1365-2958.2007.05954.x;
RA Shimada T., Hirao K., Kori A., Yamamoto K., Ishihama A.;
RT "RutR is the uracil/thymine-sensing master regulator of a set of genes for
RT synthesis and degradation of pyrimidines.";
RL Mol. Microbiol. 66:744-757(2007).
RN [7]
RP FUNCTION AS AMIDOHYDROLASE, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20400551; DOI=10.1128/jb.00201-10;
RA Kim K.S., Pelton J.G., Inwood W.B., Andersen U., Kustu S., Wemmer D.E.;
RT "The Rut pathway for pyrimidine degradation: novel chemistry and toxicity
RT problems.";
RL J. Bacteriol. 192:4089-4102(2010).
CC -!- FUNCTION: Hydrolyzes ureidoacrylate to form aminoacrylate and
CC carbamate. The carbamate hydrolyzes spontaneously, thereby releasing
CC one of the nitrogen atoms of the pyrimidine ring as ammonia and one of
CC its carbon atoms as CO2. {ECO:0000269|PubMed:16540542,
CC ECO:0000269|PubMed:20400551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-3-ureidoacrylate + H(+) + H2O = (Z)-3-aminoacrylate + CO2
CC + NH4(+); Xref=Rhea:RHEA:42624, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:59891,
CC ChEBI:CHEBI:59894; EC=3.5.1.110;
CC Evidence={ECO:0000269|PubMed:20400551};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-3-ureidoacrylate + H2O = (Z)-3-aminoacrylate + carbamate +
CC H(+); Xref=Rhea:RHEA:31603, ChEBI:CHEBI:13941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:59891, ChEBI:CHEBI:59894;
CC Evidence={ECO:0000269|PubMed:20400551};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-2-methylureidoacrylate + H(+) + H2O = (Z)-2-
CC methylaminoacrylate + CO2 + NH4(+); Xref=Rhea:RHEA:42620,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:143783, ChEBI:CHEBI:145735;
CC EC=3.5.1.110; Evidence={ECO:0000269|PubMed:20400551};
CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC called GlnG) and repressed by RutR. {ECO:0000269|PubMed:11121068,
CC ECO:0000269|PubMed:17919280}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on uridine
CC as the sole source of nitrogen at room temperature.
CC {ECO:0000269|PubMed:20400551}.
CC -!- MISCELLANEOUS: The Rut pathway degrades exogenous pyrimidines as the
CC sole nitrogen source at room temperature but not at 37 degrees Celsius,
CC a restriction that is apparently a consequence of an inadequate ability
CC to remove toxic malonic semialdehyde at the higher temperature
CC (RutE/YdfG function).
CC -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00830, ECO:0000305}.
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DR EMBL; U00096; AAC74096.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35778.1; -; Genomic_DNA.
DR PIR; A64843; A64843.
DR RefSeq; NP_415531.2; NC_000913.3.
DR RefSeq; WP_001393558.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P75897; -.
DR SMR; P75897; -.
DR BioGRID; 4261997; 1.
DR DIP; DIP-28106N; -.
DR STRING; 511145.b1011; -.
DR PaxDb; P75897; -.
DR PRIDE; P75897; -.
DR EnsemblBacteria; AAC74096; AAC74096; b1011.
DR EnsemblBacteria; BAA35778; BAA35778; BAA35778.
DR GeneID; 945699; -.
DR KEGG; ecj:JW5139; -.
DR KEGG; eco:b1011; -.
DR PATRIC; fig|511145.12.peg.1049; -.
DR EchoBASE; EB3618; -.
DR eggNOG; COG1335; Bacteria.
DR InParanoid; P75897; -.
DR OMA; WHKSNAL; -.
DR PhylomeDB; P75897; -.
DR BioCyc; EcoCyc:G6522-MON; -.
DR BioCyc; MetaCyc:G6522-MON; -.
DR BRENDA; 3.5.1.110; 2026.
DR PRO; PR:P75897; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB.
DR GO; GO:0019740; P:nitrogen utilization; IDA:UniProtKB.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IMP:EcoCyc.
DR GO; GO:0006212; P:uracil catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.850; -; 1.
DR HAMAP; MF_00830; RutB; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR019916; RutB.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
DR TIGRFAMs; TIGR03614; RutB; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..230
FT /note="Ureidoacrylate amidohydrolase RutB"
FT /id="PRO_0000201833"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:I6XD65"
FT ACT_SITE 133
FT /evidence="ECO:0000250|UniProtKB:I6XD65"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:I6XD65"
SQ SEQUENCE 230 AA; 25209 MW; 6E265222D32A6E80 CRC64;
MTTLTARPEA ITFDPQQSAL IVVDMQNAYA TPGGYLDLAG FDVSTTRPVI ANIQTAVTAA
RAAGMLIIWF QNGWDEQYVE AGGPGSPNFH KSNALKTMRK QPQLQGKLLA KGSWDYQLVD
ELVPQPGDIV LPKPRYSGFF NTPLDSILRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
GVVLEDATHQ AGPKFAQKAA LFNIETFFGW VSDVETFCDA LSPTSFAHIA
