ID   RUTC_SHIF2              Reviewed;         128 AA.
AC   D2AC41;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=SFxv_1099;
OS   Shigella flexneri serotype X (strain 2002017).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=591020;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002017;
RX   PubMed=19955273; DOI=10.1128/jcm.00614-09;
RA   Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA   Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA   Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT   "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT   clone of Shigella flexneri.";
RL   J. Clin. Microbiol. 48:419-426(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; CP001383; ADA73359.1; -; Genomic_DNA.
DR   RefSeq; WP_001126782.1; NC_017328.1.
DR   AlphaFoldDB; D2AC41; -.
DR   SMR; D2AC41; -.
DR   EnsemblBacteria; ADA73359; ADA73359; SFxv_1099.
DR   KEGG; sfe:SFxv_1099; -.
DR   PATRIC; fig|591020.3.peg.1173; -.
DR   HOGENOM; CLU_100715_7_3_6; -.
DR   OMA; MPKTIIT; -.
DR   Proteomes; UP000001884; 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_0000402768"
SQ   SEQUENCE   128 AA;  13823 MW;  275FC2374597C9DD CRC64;
     MPKSVIIPAG SSAPLAPFVP GTLADGVVYV SGTLAFDQHN NVLFADDPKA QTRHVLETIR
     KVIETAGGTM ADVTFNSIFI TDWKNYAAIN EIYAEFFPGD KPARFYIQCG LVKPDALVEI
     ATIAHIAK