Putative enzyme of alternative pyrimidine degradation pathway, putative alpha/beta hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family.

Putative luciferase family protein, putative flavin-dependent oxidoreductase; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate.

Flavin reductase domain protein, FMN-binding; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway; Belongs to the non-flavoprotein flavin reductase family. RutF subfamily.

Conserved hypothetical protein; Homologs of previously reported genes of unknown function.

Ribonuclease PH (RNase PH) (tRNA nucleotidyltransferase); Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.

Threonine deaminase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.

Putative transcriptional regulator, TetR/AcrR family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator.

Protein chain elongation factor EF-G, GTP-binding; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase f [...]

Hypothetical protein; Similar to elongation factor G (C-terminus); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor.