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Protein

Gamma-glutamyltranspeptidase 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471GlutamateBy similarity
Active sitei420 – 4201NucleophileBy similarity
Binding sitei438 – 4381GlutamateBy similarity
Binding sitei440 – 4401GlutamateBy similarity
Binding sitei459 – 4591GlutamateBy similarity
Binding sitei462 – 4621GlutamateBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular detoxification Source: PomBase
  • cellular response to oxidative stress Source: PomBase
  • glutathione catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, 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:
Gamma-glutamyltranspeptidase 2 (EC:2.3.2.2)
Alternative name(s):
Gamma-glutamyltransferase 2
Glutathione hydrolase 2 (EC:3.4.19.13)
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4242CytoplasmicSequence analysisAdd
BLAST
Transmembranei43 – 6321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini64 – 611548LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole Source: PomBase
  • 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 – 419419Gamma-glutamyltranspeptidase 2 heavy chainBy similarityPRO_0000247900Add
BLAST
Chaini420 – 611192Gamma-glutamyltranspeptidase 2 light chainBy similarityPRO_0000247901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO14194.

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 interactions.
MINTiMINT-4671272.

Structurei

3D structure databases

ProteinModelPortaliO14194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni490 – 4912Glutamate bindingBy similarity
Regioni512 – 5132Glutamate bindingBy similarity

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000175620.
InParanoidiO14194.
KOiK18592.
OMAiCENAPTI.
OrthoDBiEOG7BCNMD.
PhylomeDBiO14194.

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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO14194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279542. 6 interactions.
MINTiMINT-4671272.

Protein family/group databases

MEROPSiT03.011.

Proteomic databases

MaxQBiO14194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

HOGENOMiHOG000175620.
InParanoidiO14194.
KOiK18592.
OMAiCENAPTI.
OrthoDBiEOG7BCNMD.
PhylomeDBiO14194.

Enzyme and pathway databases

UniPathwayiUPA00204.
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.

Miscellaneous databases

PROiO14194.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a second gene encoding gamma-glutamyl transpeptidase from Schizosaccharomyces pombe."
    Park H.-J., Moon J.-S., Kim H.-G., Kim I.-H., Kim K., Park E.-H., Lim C.-J.
    Can. J. Microbiol. 51:269-275(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "The gene encoding gamma-glutamyl transpeptidase II in the fission yeast is regulated by oxidative and metabolic stress."
    Kang H.-J., Kim B.-C., Park E.-H., Ahn K., Lim C.-J.
    J. Biochem. Mol. Biol. 38:609-618(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGGT2_SCHPO
AccessioniPrimary (citable) accession number: O14194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [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

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.