RUTC_YERE8
ID RUTC_YERE8 Reviewed; 129 AA.
AC A1JMX4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=YE1948;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12027.1; -; Genomic_DNA.
DR RefSeq; YP_001006203.1; NC_008800.1.
DR AlphaFoldDB; A1JMX4; -.
DR SMR; A1JMX4; -.
DR STRING; 393305.YE1948; -.
DR EnsemblBacteria; CAL12027; CAL12027; YE1948.
DR KEGG; yen:YE1948; -.
DR PATRIC; fig|393305.7.peg.2105; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_3_6; -.
DR OMA; MPKTIIT; -.
DR Proteomes; UP000000642; 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..129
FT /note="3-aminoacrylate deaminase RutC"
FT /id="PRO_0000402770"
SQ SEQUENCE 129 AA; 13831 MW; 140B8C7C24D10138 CRC64;
MMPKTIITPP GSGTPLAPFS PGTLADGVMY VSGTLAFDKQ NNVVHIGDAA GQTRHVLETI
KSVIETAGGS LDDITFNSIF LTDWQHYAAI NQVYAEYFPG DKPARFCIQC GLVKPDALIE
IASVAHLPR