Ribonuclease PH; 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.

Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.

COGs: COG1012 NAD-dependent aldehyde dehydrogenase; InterProIPR015590:IPR001670:IPR018211:IPR016160:IPR 016162:IPR016161; KEGG: dal:Dalk_3586 aldehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; iron-containing alcohol dehydrogenase; SPTR: B8FGP4 Aldehyde Dehydrogenase; PFAM: Aldehyde dehydrogenase family; Iron-containing alcohol dehydrogenase.

Carbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...]

COGs: COG0480 Translation elongation factors (GTPase); InterProIPR000795:IPR004161:IPR005517:IPR000640:IPR 020568:IPR009000:IPR009022:IPR014721:IPR004540:IPR005225; KEGG: sfu:Sfum_0068 elongation factor G; PFAM: protein synthesis factor GTP-binding; elongation factor Tu domain 2 protein; elongation factor G domain IV; elongation factor G domain protein; SPTR: A0LEB9 Translation elongation factor G; TIGRFAM: translation elongation factor G; small GTP-binding protein; PFAM: Elongation factor Tu domain 2; Elongation factor G C-terminus; Elongation factor Tu GTP binding domain; Elongation [...]

Translation elongation factor G; 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 family. EF-G/EF-2 s [...]

Translation elongation factor G; 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 family. EF-G/EF-2 s [...]

COGs: COG2049 Allophanate hydrolase subunit 1; InterPro IPR003833:IPR003778:IPR010016; KEGG: sth:STH379 putative allophanate hydrolase; PFAM: Allophanate hydrolase subunit 1; Allophanate hydrolase subunit 2; SMART: Allophanate hydrolase subunit 1; Allophanate hydrolase subunit 2; SPTR: Q67SH9 Putative allophanate hydrolase; PFAM: Metallo-beta-lactamase superfamily; Allophanate hydrolase subunit 2; Allophanate hydrolase subunit 1; TIGRFAM: conserved hypothetical protein TIGR00370; biotin-dependent carboxylase uncharacterized domain.

DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]