ID   RUTB_PSEU2              Reviewed;         245 AA.
AC   Q4ZXR8;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Psyr_0998;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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   -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00830}.
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DR   EMBL; CP000075; AAY36054.1; -; Genomic_DNA.
DR   RefSeq; WP_011266760.1; NC_007005.1.
DR   RefSeq; YP_234092.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZXR8; -.
DR   SMR; Q4ZXR8; -.
DR   STRING; 205918.Psyr_0998; -.
DR   EnsemblBacteria; AAY36054; AAY36054; Psyr_0998.
DR   KEGG; psb:Psyr_0998; -.
DR   PATRIC; fig|205918.7.peg.1027; -.
DR   eggNOG; COG1335; Bacteria.
DR   HOGENOM; CLU_068979_8_0_6; -.
DR   OMA; WHKSNAL; -.
DR   Proteomes; UP000000426; Chromosome.
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..245
FT                   /note="Ureidoacrylate amidohydrolase RutB"
FT                   /id="PRO_0000402700"
FT   ACT_SITE        41
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT   ACT_SITE        183
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ   SEQUENCE   245 AA;  26385 MW;  A3AAD99FE8483513 CRC64;
     MTTPTTVAGV DLPDLQPARE LPARPEPLRM KPGETALVVV DMQNAYASLG GYLDLAGFDV
     SSTGPVIANI NKACAAARAA GIPVIFFQNG WDPAYVEAGG PGSPNWHKSN ALKTMRKRPE
     LEGQLLAKGG WDYQLVDELT PQPGDIVVPK IRYSGFFNSS FDSVLRSRGI RNLVFTGIAT
     NVCVESTLRD GFHLEYFGVV LADATHQAGP EFAQQAALFN IETFFGWVSS VDDFCTTFSP
     VGQPS