RUTC_SHIDS
ID RUTC_SHIDS Reviewed; 128 AA.
AC Q32HQ1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=SDY_0985;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB61154.1; -; Genomic_DNA.
DR RefSeq; WP_001126780.1; NC_007606.1.
DR RefSeq; YP_402645.1; NC_007606.1.
DR AlphaFoldDB; Q32HQ1; -.
DR SMR; Q32HQ1; -.
DR STRING; 300267.SDY_0985; -.
DR EnsemblBacteria; ABB61154; ABB61154; SDY_0985.
DR GeneID; 66670712; -.
DR KEGG; sdy:SDY_0985; -.
DR PATRIC; fig|300267.13.peg.1145; -.
DR HOGENOM; CLU_100715_7_3_6; -.
DR OMA; MPKTIIT; -.
DR Proteomes; UP000002716; 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; Reference proteome.
FT CHAIN 1..128
FT /note="3-aminoacrylate deaminase RutC"
FT /id="PRO_0000402765"
SQ SEQUENCE 128 AA; 13763 MW; 7D5FC2374597D907 CRC64;
MPKSVIIPAG SSAPLAPFVP GTLADGVVYV SGTLAFDQHN NVLFADDPKA QTRHVLETIR
KVIETAGGTM ADVTFNSIFI TDWKNYAAIN EIYAEFFPGD KPARFCIQCG LVKPDALVEI
ATIAHIAK
