RUTB_ECO1A
ID RUTB_ECO1A Reviewed; 230 AA.
AC C8UMM7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=ECO111_1200;
OS Escherichia coli O111:H- (strain 11128 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11128 / EHEC;
RX PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T.,
RA Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.;
RT "Comparative genomics reveal the mechanism of the parallel evolution of
RT O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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 ---------------------------------------------------------------------------
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; AP010960; BAI35147.1; -; Genomic_DNA.
DR RefSeq; WP_001307708.1; NC_013364.1.
DR AlphaFoldDB; C8UMM7; -.
DR SMR; C8UMM7; -.
DR EnsemblBacteria; BAI35147; BAI35147; ECO111_1200.
DR KEGG; eoi:ECO111_1200; -.
DR HOGENOM; CLU_068979_8_0_6; -.
DR OMA; WHKSNAL; -.
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_0000402668"
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; 25229 MW; 6E2647C2DB88E4A0 CRC64;
MTTLTARPEA ITFDPQQSAL IVVDMQNAYA TPGGYLDLAG FDVSTTRPVI ANIQTAVTAA
RAAGMLIIWF QNGWDEQYVE AGGPGSPNFH KSNALKTMRK QPQLQGKLLA KGSWDYQLVD
ELVPQPGDIV LPKPRYSGFF NTPLDSILRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
GVVLEDATHQ AGPEFAQKAA LFNIETFFGW VSDVETFCDA LSPTSFARIA