ID   RUTB_CAUVN              Reviewed;         238 AA.
AC   B8H1Q1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-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=CCNA_02885;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(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}.
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; CP001340; ACL96350.1; -; Genomic_DNA.
DR   RefSeq; WP_012640590.1; NC_011916.1.
DR   RefSeq; YP_002518258.1; NC_011916.1.
DR   AlphaFoldDB; B8H1Q1; -.
DR   SMR; B8H1Q1; -.
DR   EnsemblBacteria; ACL96350; ACL96350; CCNA_02885.
DR   GeneID; 7331315; -.
DR   KEGG; ccs:CCNA_02885; -.
DR   PATRIC; fig|565050.3.peg.2815; -.
DR   HOGENOM; CLU_068979_8_0_5; -.
DR   OMA; WHKSNAL; -.
DR   OrthoDB; 1442962at2; -.
DR   PhylomeDB; B8H1Q1; -.
DR   Proteomes; UP000001364; 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; Reference proteome.
FT   CHAIN           1..238
FT                   /note="Ureidoacrylate amidohydrolase RutB"
FT                   /id="PRO_0000402649"
FT   ACT_SITE        35
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        177
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ   SEQUENCE   238 AA;  25904 MW;  4C4D7C48F5699B7F CRC64;
     MSSPITPLSP GCVMLPARPE PLPVDPKTTA VIVIDMQNAY ASPGGYLDLA GFDISGAAKV
     THEIKGVLEV ARSAGMTVIY FQNGWDDGYV EAGGPGSPNW WKSNALKTMR ARPELQGKLL
     ARGQWDYELV DDLTPQPGDI RLHKTRYSGF FNSQLDSVLR ARGIRHLVFT GIATNVCVES
     TLRDGFMLEY FGTVLEDATH QAGPDFVQKA ALFNIETFFG WVSTTADFKG TFGQLAPG