Acts on thioredoxins 1 and 2.

Also known as Thioredoxin reductase 1, cytoplasmic (TR) (Gene associated with retinoic and interferon-induced mortality 12 protein) (GRIM-12) (Gene associated with retinoic and IFN-induced mortality 12 protein) (KM-102-derived reductase-like factor) (Thior.
TRXR1: a cytoplasmic pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine residue which is required for the catalytic activity.

Protein type: EC 1.8.1.9; Nuclear receptor co-regulator; Nucleotide Metabolism - pyrimidine; Oxidoreductase

Chromosomal Location of Human Ortholog: 12q23-q24.1

Cellular Component: cytosol; mitochondrion

Molecular Function: protein binding; thioredoxin-disulfide reductase activity

Biological Process: cell redox homeostasis; nucleobase, nucleoside and nucleotide interconversion; response to oxygen radical; response to reactive oxygen species; selenium metabolic process

Also known as Thioredoxin reductase 2 (NADPH-dependent thioredoxin reductase 2) (NTR2) (NADPH-dependent thioredoxin reductase A) (AtNTRA).
NADPH-dependent thioredoxin reductase, major cytosolic isoform

Also known as Thioredoxin reductase 3 (Thioredoxin and glutathione reductase) (Thioredoxin reductase TR2).
TXNRD3: Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Protein type: EC 1.8.1.9; Oxidoreductase

Chromosomal Location of Human Ortholog: 3q21.3

Cellular Component: mitochondrion

Molecular Function: thioredoxin-disulfide reductase activity

Biological Process: cell redox homeostasis; response to oxygen radical

Also known as Thioredoxin reductase gliT (Gliotoxin biosynthesis protein T).
Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). GliT is required for self-protection against gliotoxin (PubMed:20548963, PubMed:26150413). GliT plays a role in preventing dysregulation of the methyl/methionine cycle to control intracellular S-adenosylmethionine (SAM) depletion and S-adenosylhomocysteine (SAH) homeostasis during gliotoxin biosynthesis and exposure (PubMed:26150413).

Also known as Thioredoxin reductase NTRA (NADPH-dependent thioredoxin reductase A) (OsNTRA).
Possesses thioredoxin-disulfide reductase activity.

Also known as Thioredoxin reductase NTRB (NADPH-dependent thioredoxin reductase B) (OsNTRB).
Possesses thioredoxin-disulfide reductase activity.

Also known as Thioredoxin reductase NTRC (NADPH-dependent thioredoxin reductase C) (OsNTRC).
Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for the plastidial 2-Cys peroxiredoxin BAS1 and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark.

Also known as Thioredoxin reductase sirT (Sirodesmin biosynthesis protein T).
Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).

Also known as Thioredoxin reductase tcpT (Thioclapurine biosynthesis protein T).
Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catalyzed by the NRPS tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873). However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873). The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873).