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Protein

Gamma-glutamyltransferase

Gene

ECM38

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei177 – 1771GlutamateBy similarity
Active sitei470 – 4701NucleophileBy similarity
Binding sitei488 – 4881GlutamateBy similarity
Binding sitei490 – 4901GlutamateBy similarity
Binding sitei509 – 5091GlutamateBy similarity
Binding sitei512 – 5121GlutamateBy similarity

GO - Molecular functioni

  • gamma-glutamyltransferase activity Source: UniProtKB-EC
  • glutathione hydrolase activity Source: SGD

GO - Biological processi

  • glutathione catabolic process Source: SGD
  • xenobiotic metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, 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:
Gamma-glutamyltransferase (EC:2.3.2.22 Publications)
Alternative name(s):
CIK1 suppressor protein 2
Extracellular mutant protein 38
Gamma-glutamyltranspeptidase
Short name:
Gamma-GT
Glutathione hydrolase (EC:3.4.19.132 Publications)
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 660626LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Gamma-glutamyltransferase heavy chainBy similarityPRO_0000011078Add
BLAST
Chaini470 – 660191Gamma-glutamyltransferase light chainBy similarityPRO_0000011079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence analysis
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence analysis
Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence analysis
Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence analysis
Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ05902.

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. 19 interactions.
DIPiDIP-4682N.
MINTiMINT-481929.

Structurei

3D structure databases

ProteinModelPortaliQ05902.
SMRiQ05902. Positions 102-638.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni540 – 5412Glutamate bindingBy similarity
Regioni562 – 5632Glutamate bindingBy similarity

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00550000074591.
HOGENOMiHOG000175620.
InParanoidiQ05902.
KOiK00681.
OMAiDRAADFK.
OrthoDBiEOG092C24BM.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711H → R in strain: YPH499. 1 Publication
Natural varianti494 – 4941G → D in strain: YPH499; lack of gamma-glutamyl transferase activity. 1 Publication

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ05902.
SMRiQ05902. Positions 102-638.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31563. 19 interactions.
DIPiDIP-4682N.
MINTiMINT-481929.

Protein family/group databases

MEROPSiT03.012.

Proteomic databases

MaxQBiQ05902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR299W; YLR299W; YLR299W.
GeneIDi851006.
KEGGisce:YLR299W.

Organism-specific databases

EuPathDBiFungiDB:YLR299W.
SGDiS000004290. ECM38.

Phylogenomic databases

GeneTreeiENSGT00550000074591.
HOGENOMiHOG000175620.
InParanoidiQ05902.
KOiK00681.
OMAiDRAADFK.
OrthoDBiEOG092C24BM.

Enzyme and pathway databases

UniPathwayiUPA00204.
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.

Miscellaneous databases

PROiQ05902.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiECM38_YEAST
AccessioniPrimary (citable) accession number: Q05902
Secondary accession number(s): D6VYU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.