Q05902 · ECM38_YEAST

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

Activity regulation

Activity is decreased by glutathione and ammonium ion.

Pathway

Sulfur metabolism; glutathione metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site177L-glutamate (UniProtKB | ChEBI)
Active site470Nucleophile
Binding site488L-glutamate (UniProtKB | ChEBI)
Binding site490L-glutamate (UniProtKB | ChEBI)
Binding site509L-glutamate (UniProtKB | ChEBI)
Binding site512L-glutamate (UniProtKB | ChEBI)
Binding site540-541L-glutamate (UniProtKB | ChEBI)
Binding site562-563L-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentfungal-type vacuole
Cellular Componentplasma membrane
Cellular Componentvacuolar membrane
Molecular Functionglutathione hydrolase activity
Molecular Functionleukotriene C4 gamma-glutamyl transferase activity
Biological Processglutathione catabolic process
Biological Processproteolysis
Biological Processxenobiotic metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      ECM38
    • Synonyms
      CIS2
    • Ordered locus names
      YLR299W

Organism names

Accessions

  • Primary accession
    Q05902
  • Secondary accessions
    • D6VYU3

Proteomes

Organism-specific databases

Subcellular Location

Vacuole membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-13Cytoplasmic
Transmembrane14-34Helical; Signal-anchor for type II membrane protein
Topological domain35-660Lumenal

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant171in strain: YPH499
Natural variant494in strain: YPH499; lack of gamma-glutamyl transferase activity

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000110781-469Glutathione hydrolase heavy chain
Glycosylation119N-linked (GlcNAc...) asparagine
Glycosylation191N-linked (GlcNAc...) asparagine
Glycosylation270N-linked (GlcNAc...) asparagine
Glycosylation298N-linked (GlcNAc...) asparagine
Glycosylation454N-linked (GlcNAc...) asparagine
ChainPRO_0000011079470-660Glutathione hydrolase light chain
Glycosylation517N-linked (GlcNAc...) asparagine

Post-translational modification

Cleaved by autocatalysis into a large and a small subunit.

Keywords

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.

Interaction

Subunit

Heterodimer composed of a light and a heavy chain. The active site is located in the light chain.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias73-88Basic and acidic residues
Region73-92Disordered

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    660
  • Mass (Da)
    73,180
  • Last updated
    1996-11-01 v1
  • Checksum
    9896E9EBFF822F55
MLLCNRKVPKTLNTCFILHIFTLLTLGVLVSGMPSKMVSFASQETLQRINNLLRGSANRDVDIIAEYLKKDDDDDGGDKDHHNIDIDPLPRRPSLTPDRQLLKVGLHGAISSDLEVCSNLTINEVLLKFPGSNAADAAVTQALCKGMVNFFNSGIGGGGYVVFSGKDDEDHLSIDFREKAPMDSHKFMFENCSLCSKIGGLAVGVPGELMGLYRLFKERGSGQVDWRDLIEPVAKLGSVGWQIGEALGATLELYEDVFLTLKEDWSFVLNSTHDGVLKEGDWIKRPALSNMLMELAKNGSVAPFYDPDHWIAKSMIDTVAKYNGIMNLQDVSSYDVHVTKPLSMKIRKGANFIPDNDMTVLTSSGSSSGAALLAALRIMDNFQNQEGGDYEKETTYHLLESMKWMASARSRLGDFEGEALPKHIEEVLDPEWALKAVKSIKRNSQDGNFKTLENWTLYDPAYDINNPHGTAHFSIVDSHGNAVSLTTTINLLFGSLVHDPKTGVIFNNEMDDFAQFNKSNSFELAPSIYNFPEPGKRPLSSTAPTIVLSELGIPDLVVGASGGSRITTSVLQTIVRTYWYNMPILETIAYPRIHHQLLPDRIELESFPMIGKAVLSTLKEMGYTMKEVFPKSVVNAIRNVRGEWHAVSDYWRKRGISSVY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias73-88Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U17243
EMBL· GenBank· DDBJ
AAB67344.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006945
EMBL· GenBank· DDBJ
DAA09609.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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