| Antioxidant Proteins |
Accession No. |
Motif Found |
Profile |
Position in the protein |
Description |
|
APX |
Q42459 |
PEROXIDASE_2
PEROXIDASE_1 |
PEROXIDASE_4 |
33-250
33 - 44
155 - 165 |
Heme-binding peroxidases carry out a variety of biosynthetic and degradative functions using hydrogen peroxide as the electron acceptor.
They play a key role in hydrogen peroxide removal in the chloroplasts and cytosol of higher plants.
|
| Q7DN63 |
PEROXIDASE_1 |
PEROXIDASE_4
|
98 - 349
225 - 235 |
| Q41371 |
PEROXIDASE_2
PEROXIDASE_1 |
PEROXIDASE_4 |
15-256
34 - 45
147 - 157 |
| O46921 |
PEROXIDASE_1 |
PEROXIDASE_4 |
98 - 349
225 - 235 |
| Q7DN73 |
PEROXIDASE_1 |
PEROXIDASE_4 |
98 - 349
225 - 235 |
| Q7GDV4 |
PEROXIDASE_1 |
PEROXIDASE_4 |
98 - 349
225 - 235 |
| DHAR |
Q9FVE4 |
- |
GST_NTER
GST_CTER |
65 - 143
129 - 266 |
Glutathione S-transferases (GSTs) are involved in detoxification of xenobiotic compounds and in the biosynthesis of important metabolites. The N-terminal thioredoxin-like domain participate in binding the glutathione moiety via its thioredoxin-like domain while the C-terminal domain contains several hydrophobic α-helices that specifically bind hydrophobic substrates. |
| PHGPX |
O23814 |
GLUTATHIONE_PEROXID_1
GLUTATHIONE_PEROXID_2 |
GLUTATHIONE_PEROXID_3 |
2-171
32 – 47
69 - 76 |
Glutathione peroxidase is an enzyme that catalyzes the reduction of hydroxyperoxides by glutathione. Its main function is to protect against the damaging effect of endogenously formed hydroxyperoxides. |
| 2-CPs |
O24364 |
- |
THIOREDOXIN_2 |
73 - 232 |
Thioredoxins participate in various redox reactions via the reversible oxidation of an active center disulfide bond. |
