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Protein

Glutathione hydrolase proenzyme 2

Gene

ggt2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity1 Publication

Catalytic activityi

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

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 sitei147GlutamateBy similarity1
Active sitei420NucleophileBy similarity1
Binding sitei438GlutamateBy similarity1
Binding sitei440GlutamateBy similarity1
Binding sitei459GlutamateBy similarity1
Binding sitei462GlutamateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular detoxification Source: PomBase
  • cellular response to oxidative stress Source: PomBase
  • glutathione catabolic process Source: PomBase

Keywordsi

Molecular functionAcyltransferase, Hydrolase, Protease, Transferase

Enzyme and pathway databases

BRENDAi2.3.2.2. 5613.
ReactomeiR-SPO-174403. Glutathione synthesis and recycling.
R-SPO-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-SPO-5423646. Aflatoxin activation and detoxification.
UniPathwayiUPA00204.

Protein family/group databases

MEROPSiT03.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione hydrolase proenzyme 2 (EC:3.4.19.13)
Alternative name(s):
Gamma-glutamyltransferase 2
Gamma-glutamyltranspeptidase 2 (EC:2.3.2.2)
Cleaved into the following 2 chains:
Gene namesi
Name:ggt2
ORF Names:SPAC56E4.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC56E4.06c.
PomBaseiSPAC56E4.06c. ggt2.

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 – 42CytoplasmicSequence analysisAdd BLAST42
Transmembranei43 – 63Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini64 – 611LumenalSequence analysisAdd BLAST548

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002479001 – 419Glutathione hydrolase 2 heavy chainBy similarityAdd BLAST419
ChainiPRO_0000247901420 – 611Glutathione hydrolase 2 light chainBy similarityAdd BLAST192

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi396N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO14194.
PRIDEiO14194.

Expressioni

Inductioni

Induced upon nitrogen starvation and oxidative stress.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi279542. 6 interactors.
MINTiMINT-4671272.
STRINGi4896.SPAC56E4.06c.1.

Structurei

3D structure databases

ProteinModelPortaliO14194.
SMRiO14194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni490 – 491Glutamate bindingBy similarity2
Regioni512 – 513Glutamate bindingBy similarity2

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000175620.
InParanoidiO14194.
KOiK18592.
OMAiPYIHLIA.
OrthoDBiEOG092C24BM.
PhylomeDBiO14194.

Family and domain databases

InterProiView protein in InterPro
IPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiView protein in Pfam
PF01019. G_glu_transpept. 1 hit.
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O14194-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPTDTTPLL YSWDDQSRHQ DPDWHKLRNY HGAWYRRISR RRFSQFIFAF
60 70 80 90 100
GLMTLFVLVY SISSNLHTPT QFTGHKVRGR RGAVASEVPV CSDIGVSMLA
110 120 130 140 150
DGGNAVDAAI ASTFCIGVVN FFSSGIGGGG FMLIKHPNET AQSLTFREIA
160 170 180 190 200
PGNVSKHMFD KNPMLAQVGP LSIAIPGELA GLYEAWKSHG LLDWSKLLEP
210 220 230 240 250
NVKLAREGFP VTRAMERVLK LPEMAHLLKD PIWQPILMPN GKVLRAGDKM
260 270 280 290 300
FRPAYAKTLE IIANKGIEPF YRGELTNSMV KFIQDNGGIV TVEDFGNYST
310 320 330 340 350
VFADALHTSY RGHDVYTCTL PTSGPALIEG LNILDGYPLN TPSLAFPKRL
360 370 380 390 400
HLEVEAMKWL SAGRTQFGDP DFLPLDHLDV VSKLLSKEFA SQIRNNISLS
410 420 430 440 450
KTYPWEHYNP SYDLPISHGT THVSTVDSNN LAVSITSTVN LLFGSQLMDP
460 470 480 490 500
VTGVVFNDQM DDFSIPGASN AFNLSPSPWN FIEPFKRPQS SSAPTILTDI
510 520 530 540 550
NGDFEMALGA SGGSRIVTAV LDSIIKRIDM DYDIESMVAS ARPHHQLLPD
560 570 580 590 600
ILILESGFSK SVATRMKKYG HKVWRLKQHD TPLSQIQAVT RHHSEYYGMS
610
DPRKYGQAAA Y
Length:611
Mass (Da):67,825
Last modified:January 1, 1998 - v1
Checksum:i5A74721D93CC8C26
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY359853 Genomic DNA. Translation: AAQ57121.1.
CU329670 Genomic DNA. Translation: CAB16397.1.
PIRiT38908.
RefSeqiNP_593273.1. NM_001018670.2.

Genome annotation databases

EnsemblFungiiSPAC56E4.06c.1; SPAC56E4.06c.1:pep; SPAC56E4.06c.
GeneIDi2543110.
KEGGispo:SPAC56E4.06c.

Similar proteinsi

Entry informationi

Entry nameiGGT2_SCHPO
AccessioniPrimary (citable) accession number: O14194
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 1, 1998
Last modified: September 27, 2017
This is version 114 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families