ID   RUTB_ECO7I              Reviewed;         230 AA.
AC   B7NLB5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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};
GN   OrderedLocusNames=ECIAI39_2144;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928164; CAR18271.1; -; Genomic_DNA.
DR   RefSeq; WP_012602395.1; NC_011750.1.
DR   RefSeq; YP_002408107.1; NC_011750.1.
DR   AlphaFoldDB; B7NLB5; -.
DR   SMR; B7NLB5; -.
DR   STRING; 585057.ECIAI39_2144; -.
DR   EnsemblBacteria; CAR18271; CAR18271; ECIAI39_2144.
DR   KEGG; ect:ECIAI39_2144; -.
DR   PATRIC; fig|585057.6.peg.2232; -.
DR   HOGENOM; CLU_068979_8_0_6; -.
DR   OMA; WHKSNAL; -.
DR   Proteomes; UP000000749; 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..230
FT                   /note="Ureidoacrylate amidohydrolase RutB"
FT                   /id="PRO_0000402683"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ   SEQUENCE   230 AA;  25215 MW;  69257C4E965E90C6 CRC64;
     MTTLTARPEA ITFDPQQTAL IVVDMQNAYA TPGGYLDLAG FDVSTTRPVI ANIQTAVTAA
     RAAGMLIIWF QNGWDAQYVE AGGPGSPNFH KSNALKTMRK QPQLQGKLLA KGSWDYQLVD
     ELVPQPGDIV LPKPRYSSFF NTPLDSILRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
     GVVLEDATHQ AGPEFAQKAA LFNIETFFGW VSDVETFCDA LSPTSFARIA