ID   RUTC_ECOKI              Reviewed;         128 AA.
AC   D5CZH0;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=ECOK1_1062;
OS   Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=714962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHE3034 / ExPEC;
RX   PubMed=20439758; DOI=10.1073/pnas.0915077107;
RA   Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., Nesta B.,
RA   Pastorello I., Corea V.A., Torricelli G., Cartocci E., Savino S.,
RA   Scarselli M., Dobrindt U., Hacker J., Tettelin H., Tallon L.J.,
RA   Sullivan S., Wieler L.H., Ewers C., Pickard D., Dougan G., Fontana M.R.,
RA   Rappuoli R., Pizza M., Serino L.;
RT   "Identification of protective and broadly conserved vaccine antigens from
RT   the genome of extraintestinal pathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:9072-9077(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   -!- SUBUNIT: Homotrimer. {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; CP001969; ADE90297.1; -; Genomic_DNA.
DR   RefSeq; WP_001126780.1; NC_017628.1.
DR   AlphaFoldDB; D5CZH0; -.
DR   SMR; D5CZH0; -.
DR   GeneID; 66670712; -.
DR   KEGG; eih:ECOK1_1062; -.
DR   PATRIC; fig|714962.3.peg.1076; -.
DR   HOGENOM; CLU_100715_7_3_6; -.
DR   OMA; MPKTIIT; -.
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_0000402739"
SQ   SEQUENCE   128 AA;  13763 MW;  7D5FC2374597D907 CRC64;
     MPKSVIIPAG SSAPLAPFVP GTLADGVVYV SGTLAFDQHN NVLFADDPKA QTRHVLETIR
     KVIETAGGTM ADVTFNSIFI TDWKNYAAIN EIYAEFFPGD KPARFCIQCG LVKPDALVEI
     ATIAHIAK