Catalase; This enzyme is a mono-functional haem-containing catalase that acts as an antioxidant enzyme catalyzing the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects. Localized in the cytoplasm; High confidence in function and specificity.

Peroxiredoxins are thiol peroxidase involved in redox regulation of the cell. Can reduce H(2)O(2), short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox-active cysteine called the peroxidatic cysteine. It oxidized the peroxide substrate to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin; Localized in the cytoplasm; Specificity unclear.

Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity.

Ferritin; Iron-storage protein.

Co-chaperone HSP-70 protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of [...]

The long chain dehydrogenases/reductases are zinc-containing enzymes. Zinc-dependant enzymes are dimeric or tetrameric enzymes that bind two atoms of zinc per subunit where one of the zinc atom is essential for catalytic activity while the other is not. The catalytic zinc is coordinated by two cysteines and one histidine; Contains a C-terminal domain having a classical Rossman-fold that reversibly binds NAD(H); The N-terminal domain of alcohol dehydrogenase-like proteins have a GroES-like fold; Localized in the cytoplasm; Family membership.

Pseudogene; C-terminal fragment of conserved protein found in the PhnB family protein; Possibly localized in the cytoplasm; Conserved hypothetical protein.

Conserved hypothetical protein; Localized in the cytoplasm.

Thiol-disulfide oxidoreductase catalyzes the formation of disulfide bond in various substrates. Its exact specificity is not known; Belongs to the thioredoxin family; Localized in the cytoplasm; Specificity unclear.