ID RUTD_SHIF2 Reviewed; 266 AA. AC D2AC40; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 09-FEB-2010, sequence version 1. DT 19-FEB-2014, entry version 22. DE RecName: Full=Putative aminoacrylate hydrolase RutD; DE EC=3.5.1.-; DE AltName: Full=Aminohydrolase; GN Name=rutD; OrderedLocusNames=SFxv_1098; OS Shigella flexneri serotype X (strain 2002017). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 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., RA Li Z., Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., RA Luo X., Bai X., Wang Y., Wang P., Xu Q., Xu J.; RT "Emergence of a new multidrug-resistant serotype X variant in an RT epidemic clone of Shigella flexneri."; RL J. Clin. Microbiol. 48:419-426(2010). CC -!- FUNCTION: May increase the rate of spontaneous hydrolysis of CC aminoacrylate to malonic semialdehyde. Required to remove a toxic CC intermediate produce in the pyrimidine nitrogen degradation (By CC similarity). CC -!- CATALYTIC ACTIVITY: (Z)-3-aminoacrylate + H(2)O = malonate CC semialdehyde + NH(3). CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC CC also called GlnG) and repressed by RutR (Potential). CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase CC RutD family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001383; ADA73358.1; -; Genomic_DNA. DR RefSeq; YP_005726651.1; NC_017328.1. DR ProteinModelPortal; D2AC40; -. DR EnsemblBacteria; ADA73358; ADA73358; SFxv_1098. DR GeneID; 12317519; -. DR KEGG; sfe:SFxv_1098; -. DR PATRIC; 36743630; VBIShiFle60233_1172. DR HOGENOM; HOG000028072; -. DR KO; K09023; -. DR BioCyc; SFLE591020:GLK5-1089-MONOMER; -. DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro. DR GO; GO:0006212; P:uracil catabolic process; IEA:InterPro. DR HAMAP; MF_00832; RutD; 1. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR019913; Pyrimidine_utilisation_RutD. DR PRINTS; PR00111; ABHYDROLASE. DR TIGRFAMs; TIGR03611; RutD; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase. FT CHAIN 1 266 Putative aminoacrylate hydrolase RutD. FT /FTId=PRO_0000402984. SQ SEQUENCE 266 AA; 28925 MW; F538FAD4E479DE77 CRC64; MKLSLSSPPY ADAPVVVLIS GLGGSGSYWL PQLAVLEQEY QVVCYDQRGT GNNPDTLAED YSIAQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASVTMLVS VNGWLRINAH TRRCFQVRER LLYSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMPYGGHACN VTDPETFNAL LLNGLASLLH HREAAL //