ID   RUTB_CROTZ              Reviewed;         232 AA.
AC   C9Y0S6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Ctu_15920;
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX   PubMed=21037008; DOI=10.1128/jb.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
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   -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00830}.
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; FN543093; CBA29795.1; -; Genomic_DNA.
DR   RefSeq; WP_015740782.1; NC_013282.2.
DR   AlphaFoldDB; C9Y0S6; -.
DR   SMR; C9Y0S6; -.
DR   EnsemblBacteria; CBA29795; CBA29795; CTU_15920.
DR   GeneID; 60372519; -.
DR   KEGG; ctu:CTU_15920; -.
DR   PATRIC; fig|693216.3.peg.1517; -.
DR   HOGENOM; CLU_068979_8_0_6; -.
DR   OMA; WHKSNAL; -.
DR   Proteomes; UP000002069; Chromosome.
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..232
FT                   /note="Ureidoacrylate amidohydrolase RutB"
FT                   /id="PRO_0000402652"
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ   SEQUENCE   232 AA;  25387 MW;  B1752DBD7A9B23DE CRC64;
     MNAVNLMARP EALTFAPEQS ALIVVDMQNA YASQGGYLDL AGFDVSTTAP VIENIKTAVA
     AAREAGMTIV WFQNGWDSDY LEAGGPGSPN FHKSNALKTM RRRPELHGKL LAKGGWDYQL
     VDELTPLPGD IVLPKPRYSG FFNTPLDSML RARNIRHLVF TGIATNVCVE STLRDGFFLE
     YFGVVLEDAT HQAGPPFAQQ AALFNIETFF GWVSDVQRFC DALSPAALAR IA