Q05902 · ECM38_YEAST
- ProteinGlutathione hydrolase proenzyme
- GeneECM38
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids660 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation.
Miscellaneous
Present with 672 molecules/cell in log phase SD medium.
Catalytic activity
- an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]
Activity regulation
Activity is decreased by glutathione and ammonium ion.
Pathway
Sulfur metabolism; glutathione metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 177 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 470 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 488 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 490 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 509 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 512 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 540-541 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: SS | ||||||
Binding site | 562-563 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: GG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fungal-type vacuole | |
Cellular Component | plasma membrane | |
Cellular Component | vacuolar membrane | |
Molecular Function | glutathione hydrolase activity | |
Molecular Function | leukotriene C4 gamma-glutamyl transferase activity | |
Biological Process | glutathione catabolic process | |
Biological Process | proteolysis | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione hydrolase proenzyme
- EC number
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ05902
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-13 | Cytoplasmic | ||||
Sequence: MLLCNRKVPKTLN | ||||||
Transmembrane | 14-34 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TCFILHIFTLLTLGVLVSGMP | ||||||
Topological domain | 35-660 | Lumenal | ||||
Sequence: SKMVSFASQETLQRINNLLRGSANRDVDIIAEYLKKDDDDDGGDKDHHNIDIDPLPRRPSLTPDRQLLKVGLHGAISSDLEVCSNLTINEVLLKFPGSNAADAAVTQALCKGMVNFFNSGIGGGGYVVFSGKDDEDHLSIDFREKAPMDSHKFMFENCSLCSKIGGLAVGVPGELMGLYRLFKERGSGQVDWRDLIEPVAKLGSVGWQIGEALGATLELYEDVFLTLKEDWSFVLNSTHDGVLKEGDWIKRPALSNMLMELAKNGSVAPFYDPDHWIAKSMIDTVAKYNGIMNLQDVSSYDVHVTKPLSMKIRKGANFIPDNDMTVLTSSGSSSGAALLAALRIMDNFQNQEGGDYEKETTYHLLESMKWMASARSRLGDFEGEALPKHIEEVLDPEWALKAVKSIKRNSQDGNFKTLENWTLYDPAYDINNPHGTAHFSIVDSHGNAVSLTTTINLLFGSLVHDPKTGVIFNNEMDDFAQFNKSNSFELAPSIYNFPEPGKRPLSSTAPTIVLSELGIPDLVVGASGGSRITTSVLQTIVRTYWYNMPILETIAYPRIHHQLLPDRIELESFPMIGKAVLSTLKEMGYTMKEVFPKSVVNAIRNVRGEWHAVSDYWRKRGISSVY |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 171 | in strain: YPH499 | ||||
Sequence: H → R | ||||||
Natural variant | 494 | in strain: YPH499; lack of gamma-glutamyl transferase activity | ||||
Sequence: G → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000011078 | 1-469 | Glutathione hydrolase heavy chain | |||
Sequence: MLLCNRKVPKTLNTCFILHIFTLLTLGVLVSGMPSKMVSFASQETLQRINNLLRGSANRDVDIIAEYLKKDDDDDGGDKDHHNIDIDPLPRRPSLTPDRQLLKVGLHGAISSDLEVCSNLTINEVLLKFPGSNAADAAVTQALCKGMVNFFNSGIGGGGYVVFSGKDDEDHLSIDFREKAPMDSHKFMFENCSLCSKIGGLAVGVPGELMGLYRLFKERGSGQVDWRDLIEPVAKLGSVGWQIGEALGATLELYEDVFLTLKEDWSFVLNSTHDGVLKEGDWIKRPALSNMLMELAKNGSVAPFYDPDHWIAKSMIDTVAKYNGIMNLQDVSSYDVHVTKPLSMKIRKGANFIPDNDMTVLTSSGSSSGAALLAALRIMDNFQNQEGGDYEKETTYHLLESMKWMASARSRLGDFEGEALPKHIEEVLDPEWALKAVKSIKRNSQDGNFKTLENWTLYDPAYDINNPHG | ||||||
Glycosylation | 119 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 191 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 270 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 298 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 454 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000011079 | 470-660 | Glutathione hydrolase light chain | |||
Sequence: TAHFSIVDSHGNAVSLTTTINLLFGSLVHDPKTGVIFNNEMDDFAQFNKSNSFELAPSIYNFPEPGKRPLSSTAPTIVLSELGIPDLVVGASGGSRITTSVLQTIVRTYWYNMPILETIAYPRIHHQLLPDRIELESFPMIGKAVLSTLKEMGYTMKEVFPKSVVNAIRNVRGEWHAVSDYWRKRGISSVY | ||||||
Glycosylation | 517 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Cleaved by autocatalysis into a large and a small subunit.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Induced upon nitrogen starvation. Repressed by ammonium ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible inhibitors whereas serine-borate is a reversible inhibitor.
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 73-88 | Basic and acidic residues | ||||
Sequence: DDDGGDKDHHNIDIDP | ||||||
Region | 73-92 | Disordered | ||||
Sequence: DDDGGDKDHHNIDIDPLPRR |
Sequence similarities
Belongs to the gamma-glutamyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length660
- Mass (Da)73,180
- Last updated1996-11-01 v1
- Checksum9896E9EBFF822F55
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 73-88 | Basic and acidic residues | ||||
Sequence: DDDGGDKDHHNIDIDP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U17243 EMBL· GenBank· DDBJ | AAB67344.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09609.1 EMBL· GenBank· DDBJ | Genomic DNA |