A subtype of thioredoxins found primarily in CHLOROPLASTS.

Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.

Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.

A thioredoxin subtype that is ubiquitously found in the plant kingdom. It reduces a variety of seed storage proteins and may play a role in the germination process of seeds.

Deoxyribonucleic acid that makes up the genetic material of CHLOROPLASTS.

Proteins encoded by the CHLOROPLAST GENOME or proteins encoded by the nuclear genome that are imported to and resident in the CHOROPLASTS.

A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5

A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.

The genetic complement of CHLOROPLASTS as represented in their DNA.

Ribonucleic acid in chloroplasts having regulatory and catalytic roles as well as involvement in protein synthesis.