ID RUTB_ECO10 Reviewed; 230 AA.
AC C8U5H3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=ECO103_1057;
OS Escherichia coli O103:H2 (strain 12009 / EHEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585395;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12009 / 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}.
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DR EMBL; AP010958; BAI29902.1; -; Genomic_DNA.
DR RefSeq; WP_001387701.1; NC_013353.1.
DR AlphaFoldDB; C8U5H3; -.
DR SMR; C8U5H3; -.
DR KEGG; eoh:ECO103_1057; -.
DR HOGENOM; CLU_068979_8_0_6; -.
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 CDD; cd00431; cysteine_hydrolases; 1.
DR Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR HAMAP; MF_00830; RutB; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR019916; RutB.
DR NCBIfam; TIGR03614; RutB; 1.
DR PANTHER; PTHR43540:SF6; ISOCHORISMATASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43540; PEROXYUREIDOACRYLATE/UREIDOACRYLATE AMIDOHYDROLASE-RELATED; 1.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..230
FT /note="Ureidoacrylate amidohydrolase RutB"
FT /id="PRO_0000402667"
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; 6A7744E3DCF8E4A0 CRC64;
MTTLTARPEA ITFDPQQSAL IVVDMQNAYA TPGGYLDLAG FDVSTTRPVI ANIQTAVTAA
RAAGMLIIWF QNGWDEQYVE AGGPGSPNFH KSNALKTMRN QPQLQGKLLA KGSWDYQLVD
ELVPQPGDIV LPKPRYSGFF NTPLDSILRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
GVVLEDATHQ AGPEFAQKAA LFNIETFFGW VSDVETFCDA LSPTSFARIA
//
