RUTB_ECO5E
ID RUTB_ECO5E Reviewed; 231 AA.
AC B5YU52;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, 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};
GN OrderedLocusNames=ECH74115_1248;
OS Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=444450;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC4115 / EHEC;
RX PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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; CP001164; ACI39728.1; -; Genomic_DNA.
DR AlphaFoldDB; B5YU52; -.
DR SMR; B5YU52; -.
DR KEGG; ecf:ECH74115_1248; -.
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..231
FT /note="Ureidoacrylate amidohydrolase RutB"
FT /id="PRO_0000402672"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT ACT_SITE 134
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ SEQUENCE 231 AA; 25418 MW; FEDB6113E2C59577 CRC64;
MMTTLTARPE AITFDPQQSA LIVVDMQNAY ATPGGYLDLA GFDVSTTRPV IANIQTAVTA
ARAAGMLIIW FQNGWDEQYV EAGGPGSPNF HKSNALKTMR KQPQLQGKLL AKGSWDYQLV
DELVPQPGDI VLPKPRYSGF FNTPLDSILR SRGIRHLVFT SIATNVCVES TLRDGFFLEY
FGVVLEDATH QAGPEFVQKA ALFNIETFFG WVSDVETFCD ALSPTSFARI A
