ID   RUTB_ECOKI              Reviewed;         231 AA.
AC   D5CZH1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Ureidoacrylate amidohydrolase RutB {ECO:0000255|HAMAP-Rule:MF_00830};
DE            EC=3.5.1.110 {ECO:0000255|HAMAP-Rule:MF_00830};
GN   Name=rutB {ECO:0000255|HAMAP-Rule:MF_00830}; OrderedLocusNames=ECOK1_1063;
OS   Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=714962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHE3034 / ExPEC;
RX   PubMed=20439758; DOI=10.1073/pnas.0915077107;
RA   Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., Nesta B.,
RA   Pastorello I., Corea V.A., Torricelli G., Cartocci E., Savino S.,
RA   Scarselli M., Dobrindt U., Hacker J., Tettelin H., Tallon L.J.,
RA   Sullivan S., Wieler L.H., Ewers C., Pickard D., Dougan G., Fontana M.R.,
RA   Rappuoli R., Pizza M., Serino L.;
RT   "Identification of protective and broadly conserved vaccine antigens from
RT   the genome of extraintestinal pathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:9072-9077(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:0000255|HAMAP-Rule:MF_00830}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00830};
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:0000255|HAMAP-Rule:MF_00830};
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:0000255|HAMAP-Rule:MF_00830};
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC       called GlnG) and repressed by RutR. {ECO:0000255|HAMAP-Rule:MF_00830}.
CC   -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00830}.
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DR   EMBL; CP001969; ADE89592.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5CZH1; -.
DR   SMR; D5CZH1; -.
DR   KEGG; eih:ECOK1_1063; -.
DR   PATRIC; fig|714962.3.peg.1077; -.
DR   HOGENOM; CLU_068979_8_0_6; -.
DR   OMA; WHKSNAL; -.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..231
FT                   /note="Ureidoacrylate amidohydrolase RutB"
FT                   /id="PRO_0000402675"
FT   ACT_SITE        25
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        167
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ   SEQUENCE   231 AA;  25381 MW;  EF832AEBA579834B CRC64;
     MMTTLTARPE AITFDPQQTA LIVVDMQNAY ATPGGYLDLA GFDVSTTRPV IANIQTAVTA
     ARTAGMLIIW FQNGWDEQYV EAGGPGSPNY HKSNALKTMR NQPLLQGKLL AKGSWDYQLV
     DELVPQPGDI VLPKPRYSGF FNTPLDSILR SRGIRHLVFT GIATNVCVES TLRDGFFLEY
     FGVVLEDATH QAGPEFAQKA ALFNIETFFG WVSDVETFCD ALSSTSFARI A