ID C3TF03_ECOLX Unreviewed; 244 AA.
AC C3TF03;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 13-SEP-2023, entry version 60.
DE RecName: Full=Ureidoacrylate amidohydrolase RutB {ECO:0000256|HAMAP-Rule:MF_00830};
DE EC=3.5.1.110 {ECO:0000256|HAMAP-Rule:MF_00830};
GN Name=rutB {ECO:0000256|HAMAP-Rule:MF_00830};
GN ORFNames=ECs1257 {ECO:0000313|EMBL:ACI85287.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI85287.1};
RN [1] {ECO:0000313|EMBL:ACI85287.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-24 {ECO:0000313|EMBL:ACI85287.1}, 87-14
RC {ECO:0000313|EMBL:ACI85288.1}, and TW14359
RC {ECO:0000313|EMBL:ACI85290.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00830};
CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC called GlnG) and repressed by RutR. {ECO:0000256|HAMAP-Rule:MF_00830}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00830}.
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DR EMBL; EU902741; ACI85287.1; -; Genomic_DNA.
DR EMBL; EU902742; ACI85288.1; -; Genomic_DNA.
DR EMBL; EU902744; ACI85290.1; -; Genomic_DNA.
DR AlphaFoldDB; C3TF03; -.
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 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00830}.
FT DOMAIN 32..229
FT /note="Isochorismatase-like"
FT /evidence="ECO:0000259|Pfam:PF00857"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00830"
FT ACT_SITE 147
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00830"
FT ACT_SITE 180
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00830"
SQ SEQUENCE 244 AA; 26631 MW; 340B8AFC5BEBFC20 CRC64;
MPRPSPCADS GGGMMTTLTA RPEAITFDPQ QSALIVVDMQ NAYATPGGYL DLAGFDVSTT
RPVIANIQTA VTAARAAGML IIWFQNGWDE QYVEAGGPGS PNFHKSNALK TMRKQPQLQG
KLLAKGSWDY QLVDELVPQP GDIVLPKPRY SGFFNTPLDS ILRSRGIRHL VFTSIATNVC
VESTLRDGFF LEYFGVVLED ATHQAGPEFV QKAALFNIET FFGWVSDVET FCDALSPTSF
ARIA
//
