AC   MF_00830;
DC   Protein; auto
TR   HAMAP; MF_00830; -; 1; level=0
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Names: RutB
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ID   RUTB
DE   RecName: Full=Ureidoacrylate amidohydrolase RutB;
DE            EC=3.5.1.110;
GN   Name=rutB;
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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.
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;
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   -!- 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;
case <OC:Escherichia> or <OC:Shigella>
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC       called GlnG) and repressed by RutR.
end case
CC   -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
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DR   Pfam; PF00857; Isochorismatase; 1; trigger=no
DR   NCBIfam; TIGR03614; RutB; 1; trigger=no
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KW   Hydrolase
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GO   GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO   GO:0006212; P:uracil catabolic process
GO   GO:0019740; P:nitrogen utilization
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FT   From: RUTB_ECOLI (P75897)
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT   Condition: D
FT   ACT_SITE        133
FT   Condition: K
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT   Condition: C
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Size: 225-258;
Related: None;
Template: P75897;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.12 2023/06/01
//