P40582
Gene name |
GTT1 (YIR038C) |
Protein name |
Glutathione S-transferase 1 |
Names |
GST-I |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YIR038C |
EC number |
2.5.1.18: Transferring alkyl or aryl groups, other than methyl groups |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P40582
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P40582-F1 | Predicted | AlphaFoldDB |
2 variants for P40582
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s09-424066 | 149 | Q>E | No | SGRP | |
| s09-424024 | 163 | V>L | No | SGRP |
No associated diseases with P40582
1 regional properties for P40582
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | UDP-glycosyltransferase family, conserved site | 324 - 367 | IPR035595 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.5.1.18 | Transferring alkyl or aryl groups, other than methyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell periphery | The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| mitochondrial outer membrane | The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| glutathione peroxidase activity | Catalysis of the reaction: 2 glutathione + hydrogen peroxide = oxidized glutathione + 2 H2O. |
| glutathione transferase activity | Catalysis of the reaction: R-X + glutathione = H-X + R-S-glutathione. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glutathione metabolic process | The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle. |
| protein glutathionylation | The protein modification process in which a glutathione molecule is added to a protein amino acid through a disulfide linkage. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSLPIIKVHW | LDHSRAFRLL | WLLDHLNLEY | EIVPYKRDAN | FRAPPELKKI | HPLGRSPLLE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VQDRETGKKK | ILAESGFIFQ | YVLQHFDHSH | VLMSEDADIA | DQINYYLFYV | EGSLQPPLMI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EFILSKVKDS | GMPFPISYLA | RKVADKISQA | YSSGEVKNQF | DFVEGEISKN | NGYLVDGKLS |
| 190 | 200 | 210 | 220 | 230 | |
| GADILMSFPL | QMAFERKFAA | PEDYPAISKW | LKTITSEESY | AASKEKARAL | GSNF |