| IED ID | IndEnz0002018505 |
| Enzyme Type ID | protease018505 |
| Protein Name |
Glutathione hydrolase proenzyme 1 EC 3.4.19.13 Gamma-glutamyltransferase 1 Gamma-glutamyltranspeptidase 1 EC 2.3.2.2 Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain |
| Gene Name | ggt1 SPAC664.09 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MGINTSSAQSSGAASIARSSVNVKSGNRHLSSNKKSATSALEERASRPSILVTFLVLAGTILSLYIWPILSPDLFFANQRCSFKYKNKGSQRVVVEGKNGVVATEEETCSQIGVGILKAGGNAVDAAIASGICIGAVNSFSSGIGGGGFMLIRHPNGTAHSLNFRETAPAGASKNMFHGNSTLSQVGGLSVAVPGEIAGYERAWKMYGSLPWHKLFEPTIRLMRDGMPMPKELASRIRRPEFSYFKTHPDWSKIFAPEGVFLHVGEKFYRPALASTLEEIAKFGPEVFYTGKIAERLVKFVQQQGGILTMEDMANFSVVVEEPIYGNFYDREVITCGSPCSGEALILGLNVLSKVDLSEGTSILGCEMTDIGVHHLIETMKWMSAGRTVLADPTFYNNTDHVEQLLSLEYADEIRNNISNERTFDFTHYKAEYDFPNDHGTTHLSVIDKDNMAVGLTASINLMFGSQLLEPETGIILNDHMDDFASPGIVNAFGLSPSPYNFIAPGKRPQSSAVPTILVYNGEVEMVLGGSGGSRIVTAVLDTIIKKYKWGKSLLESVESPRFHHQLMPNIVYIDETVEIEVLRALEKFGHIVDLIPVQYPFSEIQAVFRTNGTLYGLSDSRKQAVAAAY |
| Enzyme Length | 630 |
| Uniprot Accession Number | Q9US04 |
| Absorption | |
| Active Site | ACT_SITE 441; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 165; /note=Glutamate; /evidence=ECO:0000250; BINDING 459; /note=Glutamate; /evidence=ECO:0000250; BINDING 461; /note=Glutamate; /evidence=ECO:0000250; BINDING 483; /note=Glutamate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; CATALYTIC ACTIVITY: Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779, ChEBI:CHEBI:143103; EC=3.4.19.13; |
| DNA Binding | |
| EC Number | 3.4.19.13; 2.3.2.2 |
| Enzyme Function | FUNCTION: Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. {ECO:0000269|PubMed:15052323}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Sulfur metabolism; glutathione metabolism. |
| nucleotide Binding | |
| Features | Active site (1); Binding site (4); Chain (2); Glycosylation (6); Region (2); Topological domain (2); Transmembrane (1) |
| Keywords | Acyltransferase;Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: Induced upon nitrogen starvation. Also induced by non-fermentable carbon sources such as glycerol, acetate and ethanol in a pap1-independent manner. {ECO:0000269|PubMed:15765057}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20473289; 22633491; 23697806; 25720772; 29996109; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,722 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:23904; RHEA:28807; RHEA:59468 |
| Cross Reference Brenda |