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 [...]

PFAM: Uncharacterised conserved protein UCP029693; KEGG: mmw:Mmwyl1_2978 hypothetical protein.

TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: mmw:Mmwyl1_2592 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial.

SMART: ATPase, AAA+ type, core; TIGRFAM: Glycine betaine/L-proline transport ATP-binding subunit; KEGG: ppr:PBPRB1788 putative glycine betaine ABC transporter ATP-binding protein; PFAM: ABC transporter-like.

ABC-type transporter, integral membrane subunit; PFAM: Binding-protein-dependent transport systems inner membrane component; KEGG: vha:VIBHAR_06563 glycine betaine/L-proline ABC transporter permease protein.

Putative signal transduction protein; PFAM: Metal-dependent hydrolase HDOD; KEGG: mmw:Mmwyl1_3755 putative signal transduction protein.

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. In the C-terminal section; belongs to the NnrD/CARKD family.

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 [...]