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Protein

Glutathione hydrolase proenzyme

Gene

ECM38

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

Miscellaneous

Present with 672 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.2 Publications
Glutathione + H2O = L-cysteinylglycine + L-glutamate.2 Publications

Enzyme regulationi

Activity is decreased by glutathione and ammonium ion.1 Publication

Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei177GlutamateBy similarity1
Active sitei470NucleophileBy similarity1
Binding sitei488GlutamateBy similarity1
Binding sitei490GlutamateBy similarity1
Binding sitei509GlutamateBy similarity1
Binding sitei512GlutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • glutathione catabolic process Source: SGD
  • xenobiotic metabolic process Source: SGD

Keywordsi

Molecular functionAcyltransferase, Hydrolase, Protease, Transferase

Enzyme and pathway databases

BioCyciYEAST:YLR299W-MONOMER
ReactomeiR-SCE-174403 Glutathione synthesis and recycling
R-SCE-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-SCE-5423646 Aflatoxin activation and detoxification
UniPathwayiUPA00204

Protein family/group databases

MEROPSiT03.012

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione hydrolase proenzyme (EC:3.4.19.132 Publications)
Alternative name(s):
CIK1 suppressor protein 2
Extracellular mutant protein 38
Gamma-glutamyltransferase (EC:2.3.2.22 Publications)
Gamma-glutamyltranspeptidase
Short name:
Gamma-GT
Cleaved into the following 2 chains:
Gene namesi
Name:ECM38
Synonyms:CIS2
Ordered Locus Names:YLR299W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR299W
SGDiS000004290 ECM38

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13CytoplasmicSequence analysisAdd BLAST13
Transmembranei14 – 34Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini35 – 660LumenalSequence analysisAdd BLAST626

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000110781 – 469Glutathione hydrolase heavy chainBy similarityAdd BLAST469
ChainiPRO_0000011079470 – 660Glutathione hydrolase light chainBy similarityAdd BLAST191

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi191N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi270N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi298N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi454N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi517N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ05902
PaxDbiQ05902
PRIDEiQ05902

Expressioni

Inductioni

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.4 Publications

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi31563, 36 interactors
DIPiDIP-4682N
MINTiQ05902
STRINGi4932.YLR299W

Structurei

3D structure databases

ProteinModelPortaliQ05902
SMRiQ05902
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni540 – 541Glutamate bindingBy similarity2
Regioni562 – 563Glutamate bindingBy similarity2

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074591
HOGENOMiHOG000175620
InParanoidiQ05902
KOiK00681
OMAiTKNMFLD
OrthoDBiEOG092C24BM

Family and domain databases

InterProiView protein in InterPro
IPR000101 GGT_peptidase
IPR029055 Ntn_hydrolases_N
PANTHERiPTHR11686 PTHR11686, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
TIGRFAMsiTIGR00066 g_glut_trans, 1 hit
PROSITEiView protein in PROSITE
PS00462 G_GLU_TRANSPEPTIDASE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLCNRKVPK TLNTCFILHI FTLLTLGVLV SGMPSKMVSF ASQETLQRIN
60 70 80 90 100
NLLRGSANRD VDIIAEYLKK DDDDDGGDKD HHNIDIDPLP RRPSLTPDRQ
110 120 130 140 150
LLKVGLHGAI SSDLEVCSNL TINEVLLKFP GSNAADAAVT QALCKGMVNF
160 170 180 190 200
FNSGIGGGGY VVFSGKDDED HLSIDFREKA PMDSHKFMFE NCSLCSKIGG
210 220 230 240 250
LAVGVPGELM GLYRLFKERG SGQVDWRDLI EPVAKLGSVG WQIGEALGAT
260 270 280 290 300
LELYEDVFLT LKEDWSFVLN STHDGVLKEG DWIKRPALSN MLMELAKNGS
310 320 330 340 350
VAPFYDPDHW IAKSMIDTVA KYNGIMNLQD VSSYDVHVTK PLSMKIRKGA
360 370 380 390 400
NFIPDNDMTV LTSSGSSSGA ALLAALRIMD NFQNQEGGDY EKETTYHLLE
410 420 430 440 450
SMKWMASARS RLGDFEGEAL PKHIEEVLDP EWALKAVKSI KRNSQDGNFK
460 470 480 490 500
TLENWTLYDP AYDINNPHGT AHFSIVDSHG NAVSLTTTIN LLFGSLVHDP
510 520 530 540 550
KTGVIFNNEM DDFAQFNKSN SFELAPSIYN FPEPGKRPLS STAPTIVLSE
560 570 580 590 600
LGIPDLVVGA SGGSRITTSV LQTIVRTYWY NMPILETIAY PRIHHQLLPD
610 620 630 640 650
RIELESFPMI GKAVLSTLKE MGYTMKEVFP KSVVNAIRNV RGEWHAVSDY
660
WRKRGISSVY
Length:660
Mass (Da):73,180
Last modified:November 1, 1996 - v1
Checksum:i9896E9EBFF822F55
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti171H → R in strain: YPH499. 1 Publication1
Natural varianti494G → D in strain: YPH499; lack of gamma-glutamyl transferase activity. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17243 Genomic DNA Translation: AAB67344.1
BK006945 Genomic DNA Translation: DAA09609.1
PIRiS50383
RefSeqiNP_013402.1, NM_001182187.1

Genome annotation databases

EnsemblFungiiYLR299W; YLR299W; YLR299W
GeneIDi851006
KEGGisce:YLR299W

Similar proteinsi

Entry informationi

Entry nameiECM38_YEAST
AccessioniPrimary (citable) accession number: Q05902
Secondary accession number(s): D6VYU3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health