ID   RUTC_ENTCC              Reviewed;         128 AA.
AC   D5CE34;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=3-aminoacrylate deaminase RutC {ECO:0000255|HAMAP-Rule:MF_00831};
DE            Short=3-AA deaminase {ECO:0000255|HAMAP-Rule:MF_00831};
DE            EC=3.5.-.- {ECO:0000255|HAMAP-Rule:MF_00831};
GN   Name=rutC {ECO:0000255|HAMAP-Rule:MF_00831}; OrderedLocusNames=ECL_02624;
OS   Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC
OS   13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=716541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC
RC   279-56;
RX   PubMed=20207761; DOI=10.1128/jb.00067-10;
RA   Ren Y., Ren Y., Zhou Z., Guo X., Li Y., Feng L., Wang L.;
RT   "Complete genome sequence of Enterobacter cloacae subsp. cloacae type
RT   strain ATCC 13047.";
RL   J. Bacteriol. 192:2463-2464(2010).
CC   -!- FUNCTION: Involved in pyrimidine catabolism. Catalyzes the deamination
CC       of 3-aminoacrylate to malonic semialdehyde, a reaction that can also
CC       occur spontaneously. RutC may facilitate the reaction and modulate the
CC       metabolic fitness, rather than catalyzing essential functions.
CC       {ECO:0000255|HAMAP-Rule:MF_00831}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(Z)-3-aminoacrylate + H(+) + H2O = 3-oxopropanoate + NH4(+);
CC         Xref=Rhea:RHEA:34947, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:33190, ChEBI:CHEBI:59894;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00831};
CC   -!- SIMILARITY: Belongs to the RutC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00831}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001918; ADF62167.1; -; Genomic_DNA.
DR   RefSeq; WP_013097195.1; NC_014121.1.
DR   RefSeq; YP_003613116.1; NC_014121.1.
DR   AlphaFoldDB; D5CE34; -.
DR   SMR; D5CE34; -.
DR   STRING; 716541.ECL_02624; -.
DR   EnsemblBacteria; ADF62167; ADF62167; ECL_02624.
DR   GeneID; 60929720; -.
DR   KEGG; enc:ECL_02624; -.
DR   PATRIC; fig|716541.4.peg.2797; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_100715_7_3_6; -.
DR   OMA; MPKTIIT; -.
DR   Proteomes; UP000002363; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; 3.30.1330.40; -; 1.
DR   HAMAP; MF_00831; RutC; 1.
DR   InterPro; IPR019897; RidA_CS.
DR   InterPro; IPR019898; RutC.
DR   InterPro; IPR035959; RutC-like_sf.
DR   InterPro; IPR006175; YjgF/YER057c/UK114.
DR   PANTHER; PTHR11803; PTHR11803; 1.
DR   Pfam; PF01042; Ribonuc_L-PSP; 1.
DR   SUPFAM; SSF55298; SSF55298; 1.
DR   TIGRFAMs; TIGR03610; RutC; 1.
DR   PROSITE; PS01094; UPF0076; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..128
FT                   /note="3-aminoacrylate deaminase RutC"
FT                   /id="PRO_0000402718"
SQ   SEQUENCE   128 AA;  13839 MW;  AE0BD725A0787600 CRC64;
     MPKSVIIPPG TSTPIAPFVP GTLADGVVYV SGTLPFDKDN NVVFINDPKA QTRHVLETIK
     TVIETAGGTM EDVTFNSIFI TDWKNYAAIN EIYAEFFPGD KPARFCIQCG LVKPDALVEI
     ATVAHIGK