ID RUTB_ECOD1 Reviewed; 230 AA.
AC C9QZ65; E6P340;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 27-MAR-2024, entry version 65.
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=EcDH1_2631, ECDH1ME8569_0965;
OS Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIMB 12045 / K12 / DH1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=536056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33849 / DSM 4235 / NCIMB 12045 / K12 / DH1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Keasling J.D.;
RT "Complete sequence of Escherichia coli DH1.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33849 / DSM 4235 / NCIMB 12045 / K12 / DH1;
RX PubMed=21611185; DOI=10.1371/journal.pone.0019534;
RA Suzuki S., Ono N., Furusawa C., Ying B.W., Yomo T.;
RT "Comparison of sequence reads obtained from three next-generation
RT sequencing platforms.";
RL PLoS ONE 6:E19534-E19534(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACX40265.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP001637; ACX40265.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP012030; BAJ42821.1; -; Genomic_DNA.
DR RefSeq; WP_001393558.1; NC_017638.1.
DR AlphaFoldDB; C9QZ65; -.
DR SMR; C9QZ65; -.
DR KEGG; edh:EcDH1_2631; -.
DR KEGG; edj:ECDH1ME8569_0965; -.
DR PATRIC; fig|536056.19.peg.1022; -.
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_0000402657"
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; 25209 MW; 6E265222D32A6E80 CRC64;
MTTLTARPEA ITFDPQQSAL IVVDMQNAYA TPGGYLDLAG FDVSTTRPVI ANIQTAVTAA
RAAGMLIIWF QNGWDEQYVE AGGPGSPNFH KSNALKTMRK QPQLQGKLLA KGSWDYQLVD
ELVPQPGDIV LPKPRYSGFF NTPLDSILRS RGIRHLVFTG IATNVCVEST LRDGFFLEYF
GVVLEDATHQ AGPKFAQKAA LFNIETFFGW VSDVETFCDA LSPTSFAHIA
//
