ID   RUTC_CROTZ              Reviewed;         132 AA.
AC   C9Y0S5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=Ctu_15910;
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX   PubMed=21037008; DOI=10.1128/jb.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
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}.
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DR   EMBL; FN543093; CBA29793.1; -; Genomic_DNA.
DR   RefSeq; WP_015740781.1; NC_013282.2.
DR   AlphaFoldDB; C9Y0S5; -.
DR   SMR; C9Y0S5; -.
DR   EnsemblBacteria; CBA29793; CBA29793; CTU_15910.
DR   GeneID; 60372797; -.
DR   KEGG; ctu:CTU_15910; -.
DR   PATRIC; fig|693216.3.peg.1516; -.
DR   HOGENOM; CLU_100715_7_3_6; -.
DR   OMA; MPKTIIT; -.
DR   Proteomes; UP000002069; 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..132
FT                   /note="3-aminoacrylate deaminase RutC"
FT                   /id="PRO_0000402717"
SQ   SEQUENCE   132 AA;  14068 MW;  F32F53D93AF46158 CRC64;
     MPKQVIIPPG ASTPIAPFVP GTLADGVVYV SGTLPFDKAN NVVYPGDPKA QTRHVLETIR
     HVIETAGGTM EDVTFNSIFI TDWKNYAAIN EIYAEFFPGD KPARFCIQCG LVKPEALVEI
     ATVAHIGPSG GA