ID   RUTB_ENTCC              Reviewed;         229 AA.
AC   D5CE33;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=ECL_02623;
OS   Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS   13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=716541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC   279-56;
RX   PubMed=20207761; DOI=10.1128/jb.00067-10;
RA   Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT   "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT   strain ATCC 13047.";
RL   J. Bacteriol. 192:2463-2464(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   -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00830}.
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DR   EMBL; CP001918; ADF62166.1; -; Genomic_DNA.
DR   RefSeq; WP_013097194.1; NC_014121.1.
DR   RefSeq; YP_003613115.1; NC_014121.1.
DR   AlphaFoldDB; D5CE33; -.
DR   SMR; D5CE33; -.
DR   STRING; 716541.ECL_02623; -.
DR   EnsemblBacteria; ADF62166; ADF62166; ECL_02623.
DR   GeneID; 60929721; -.
DR   KEGG; enc:ECL_02623; -.
DR   PATRIC; fig|716541.4.peg.2796; -.
DR   eggNOG; COG1335; Bacteria.
DR   HOGENOM; CLU_068979_8_0_6; -.
DR   OMA; WHKSNAL; -.
DR   Proteomes; UP000002363; 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..229
FT                   /note="Ureidoacrylate amidohydrolase RutB"
FT                   /id="PRO_0000402653"
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   229 AA;  24957 MW;  3E2B6D47C53BF87D CRC64;
     MTTLNARPEA ITFSAPQSAL IVVDMQNAYA SPGGYLDLAG FDVSATRPVI ENIKTAVAAA
     RAAGMLIIWF QNGWDDQYVE AGGPGSPNFH KSNALKTMRK RPELQGKLLA KGGWDYQLVD
     ELVPEAGDIV LPKPRYSGFF NTPLDSLLRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
     GVVLEDATHQ AGPEFAQKAA LFNIETFFGW VSNVADFCDA LNPPLARIA