25-diketo-D-gluconic acid reductase B (EC 1.1.1.274) (25-DKG reductase B) (25-DKGR B) (25DKGR-B) (AKR5D). TREMBL:Q8Y090: 67% identity, 78% similarity. Catalyzes the reduction of 25-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG) (By similarity). subunit:monomer (by similarity). subcellular location:cytoplasmic (by similarity). 2-keto-l-gulonic acid is a key intermediate in the production of l-ascorbic acid (vitamin c). belongs to the aldo/keto reductase family InterPro:IPR001395; Aldo/ket_red. Pfam:PF00248; aldo_ket_red; 1. PRINTS PR00069; ALDKETRDTAS ribH: riboflavin sy [...]

Probable transcriptional regulator, LysR family,; Family membership; Belongs to the LysR transcriptional regulatory family.

Conserved hypothetical secreted protein: Homology to ne0129 of N. europaea of 43% (trembl|Q82XW6). Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. signal peptide. no TMHs; Conserved hypothetical protein.

Putative catalase; Serves to protect cells from the toxic effects of hydrogen peroxide.

Conserved hypothetical secreted protein. Homology to bb3588 of B. bronchiseptica of 41% (trembl|Q7WGK1). Smart: Bacterial OsmY and nodulation domain (BON). The BON domain is typically ~60 residues long and has an alpha/beta predicted fold. There is a conserved glycine residue and several hydrophobic regions. This pattern of conservation is more suggestive of a binding or structural function rather than a catalytic function. Most proteobacteria seem to possess one or two BON-containing proteins, typically of the OsmY-type proteins. signal peptide. TMH in signal peptide; Conserved hypoth [...]

NAD(+) synthase (glutamine-hydrolyzing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.

Conserved hypothetical protein, 43% identity (60% similarity) to TrEMBL; Q8ZML9. TrEMBL;Q8X937(44% identity to Escherichia coli) Has PF04972, Putative phospholipid-binding domain;IPR007055, TAD; This domain is found in a family of osmotic shock protection proteins (e.g. P27291). It is also found in some Secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. Has SMART;SM00257,LysM, Lysin motif:IPR002482; This domain is about 40 residues long and is found in a variety of enzymes involved in bacterial cell wall degradation. This domain [...]

Conserved hypothetical 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 the repair o [...]

Gluconolactonase precursor (D-glucono-delta-lactone lactonohydrolase).HYDROLYZES THE GLUCONOLACTONE FORMED BY GLUCOSE-FRUCTOSE OXIDOREDUCTASE AND THAT FORMED IN AEROBIC CONDITIONS BY THE GLUCOSE DEHYDROGENASE PRESENT. 30% SMP-30. Pfam:PF03758; SMP-30; 1. Signal peptide: present; High confidence in function and specificity.