| IED ID | IndEnz0018000963 |
| Enzyme Type ID | peroxidase000963 |
| Protein Name |
Glutathione S-transferase EC 2.5.1.18 GST class-alpha Cleaved into: Glutathione S-transferase, N-terminally processed |
| Gene Name | |
| Organism | Antechinus stuartii (Brown marsupial mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Metatheria Dasyuromorphia Dasyuridae Antechinus (broad-footed marsupial mice) Antechinus stuartii (Brown marsupial mouse) |
| Enzyme Sequence | MAGEQNIKYFNIKGRMEAIRWLLAVAGVEFEEKFFETKEQLQKLKETVLLFQQVPMVEIDGMKLVQTRAILHYIAEKYNLLGKDMKEHAQIIMYSEGTMDLMELIMIYPFLKGEEKKQRLVEIANKAKGRYFPAFENVLKTHGQNFLVGNQLSMADVQLFEAILMVEEKVPDALSGFPLLQAFKTRISNIPTVKTFLAPGSKRKPVPDAKYVEDIIKIFYF |
| Enzyme Length | 221 |
| Uniprot Accession Number | P80894 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 9; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P13745; BINDING 45; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P13745 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133768; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889; Evidence={ECO:0000250|UniProtKB:P08263}; CATALYTIC ACTIVITY: Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione; Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865; Evidence={ECO:0000250|UniProtKB:P08263};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937; Evidence={ECO:0000250|UniProtKB:P08263}; |
| DNA Binding | |
| EC Number | 2.5.1.18 |
| Enzyme Function | FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid. {ECO:0000250|UniProtKB:P08263}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (2); Chain (2); Domain (2); Initiator methionine (1); Modified residue (2); Region (2) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000269|PubMed:9109421"; MOD_RES 2; /note="N-acetylalanine; in Glutathione S-transferase, N-terminally processed"; /evidence="ECO:0000250|UniProtKB:P30115" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,534 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16437; RHEA:16438; RHEA:50796; RHEA:50797; RHEA:50804; RHEA:50805; RHEA:48888; RHEA:48889; RHEA:43936; RHEA:43937 |
| Cross Reference Brenda |