ID   RUTB_ECOBD              Reviewed;         230 AA.
AC   C6EHJ6; C5W2X0; C6VAT9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
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=ECBD_2583, ECD_01014, B21_01021;
OS   Escherichia coli (strain B / BL21-DE3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=469008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.;
RT   "Sequencing and gene expression analysis of Escherichia coli BL21.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT   "Complete sequence of Escherichia coli BL21(DE3).";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RX   PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA   Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A.,
RA   Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B.,
RA   Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.;
RT   "Genome sequences of Escherichia coli B strains REL606 and BL21(DE3).";
RL   J. Mol. Biol. 394:644-652(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACT29605.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ACT42909.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AM946981; CAQ31538.1; -; Genomic_DNA.
DR   EMBL; CP001665; ACT29605.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001509; ACT42909.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001307100.1; NZ_CP053602.1.
DR   AlphaFoldDB; C6EHJ6; -.
DR   SMR; C6EHJ6; -.
DR   STRING; 469008.B21_01021; -.
DR   KEGG; ebd:ECBD_2583; -.
DR   KEGG; ebe:B21_01021; -.
DR   KEGG; ebl:ECD_01014; -.
DR   PATRIC; fig|469008.15.peg.1036; -.
DR   eggNOG; COG1335; Bacteria.
DR   HOGENOM; CLU_068979_8_0_6; -.
DR   OMA; WHKSNAL; -.
DR   Proteomes; UP000002032; 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_0000402660"
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;  25210 MW;  6E265222DB88E4A0 CRC64;
     MTTLTARPEA ITFDPQQSAL IVVDMQNAYA TPGGYLDLAG FDVSTTRPVI ANIQTAVTAA
     RAAGMLIIWF QNGWDEQYVE AGGPGSPNFH KSNALKTMRK QPQLQGKLLA KGSWDYQLVD
     ELVPQPGDIV LPKPRYSGFF NTPLDSILRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
     GVVLEDATHQ AGPEFAQKAA LFNIETFFGW VSDVETFCDA LSPTSFAHIA