RUTB_METEP
ID RUTB_METEP Reviewed; 248 AA.
AC A9W3I0;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Mext_1737;
OS Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=419610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Marx C., Richardson P.;
RT "Complete sequence of Methylobacterium extorquens PA1.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000908; ABY30136.1; -; Genomic_DNA.
DR RefSeq; WP_012253316.1; NC_010172.1.
DR AlphaFoldDB; A9W3I0; -.
DR SMR; A9W3I0; -.
DR STRING; 419610.Mext_1737; -.
DR EnsemblBacteria; ABY30136; ABY30136; Mext_1737.
DR KEGG; mex:Mext_1737; -.
DR eggNOG; COG1335; Bacteria.
DR HOGENOM; CLU_068979_8_0_5; -.
DR OMA; WHKSNAL; -.
DR BioCyc; MEXT419610:MEXT_RS08815-MON; -.
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..248
FT /note="Ureidoacrylate amidohydrolase RutB"
FT /id="PRO_0000402694"
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 248 AA; 26831 MW; B4F3647DE5EDC63F CRC64;
MDADAPAGYR DPSGRHGAVT LPARPEPVAF DADATVLIVV DMQNAYATKG GYLDLAGFDV
SATGPVIERI ARAVAAARAA GIRVVWFQNG WDPDYVEAGG PGSPNWHKSN ALKTMRRRPE
MNQRLLAKGT WDYALVDALT PEPGDIVLPK PRYSGFYNTP LDSMLRARGI RTLVFTGIAT
NVCVESTLRD GYHREYFGIV LADATHQAGP PALQEGALRN IETFFGWVSD VAAFEAALSS
DEARRIPA