GGT2_SCHPO
ID GGT2_SCHPO Reviewed; 611 AA.
AC O14194;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutathione hydrolase proenzyme 2;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltransferase 2;
DE AltName: Full=Gamma-glutamyltranspeptidase 2;
DE EC=2.3.2.2 {ECO:0000305|PubMed:15920625};
DE Contains:
DE RecName: Full=Glutathione hydrolase 2 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 2 light chain;
DE Flags: Precursor;
GN Name=ggt2; ORFNames=SPAC56E4.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15920625; DOI=10.1139/w04-137;
RA Park H.-J., Moon J.-S., Kim H.-G., Kim I.-H., Kim K., Park E.-H.,
RA Lim C.-J.;
RT "Characterization of a second gene encoding gamma-glutamyl transpeptidase
RT from Schizosaccharomyces pombe.";
RL Can. J. Microbiol. 51:269-275(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP INDUCTION.
RX PubMed=16202243; DOI=10.5483/bmbrep.2005.38.5.609;
RA Kang H.-J., Kim B.-C., Park E.-H., Ahn K., Lim C.-J.;
RT "The gene encoding gamma-glutamyl transpeptidase II in the fission yeast is
RT regulated by oxidative and metabolic stress.";
RL J. Biochem. Mol. Biol. 38:609-618(2005).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the transfer of the gamma-glutamyl moiety of
CC glutathione (GSH) and other gamma-glutamyl compounds to amino acids and
CC peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release
CC of L-glutamate from GSH. Plays a role in the turnover of the vacuolar
CC GSH, serving as an alternative nitrogen source during nitrogen
CC starvation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15920625}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2;
CC Evidence={ECO:0000305|PubMed:15920625};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC site is located in the light chain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced upon nitrogen starvation and oxidative stress.
CC {ECO:0000269|PubMed:16202243}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY359853; AAQ57121.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16397.1; -; Genomic_DNA.
DR PIR; T38908; T38908.
DR RefSeq; NP_593273.1; NM_001018670.2.
DR AlphaFoldDB; O14194; -.
DR SMR; O14194; -.
DR BioGRID; 279542; 8.
DR STRING; 4896.SPAC56E4.06c.1; -.
DR MEROPS; T03.011; -.
DR iPTMnet; O14194; -.
DR MaxQB; O14194; -.
DR PaxDb; O14194; -.
DR EnsemblFungi; SPAC56E4.06c.1; SPAC56E4.06c.1:pep; SPAC56E4.06c.
DR GeneID; 2543110; -.
DR KEGG; spo:SPAC56E4.06c; -.
DR PomBase; SPAC56E4.06c; ggt2.
DR VEuPathDB; FungiDB:SPAC56E4.06c; -.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_0_1; -.
DR InParanoid; O14194; -.
DR OMA; LAPGKRC; -.
DR PhylomeDB; O14194; -.
DR BRENDA; 2.3.2.2; 5613.
DR Reactome; R-SPO-174403; Glutathione synthesis and recycling.
DR Reactome; R-SPO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-SPO-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-SPO-9753281; Paracetamol ADME.
DR UniPathway; UPA00204; -.
DR PRO; PR:O14194; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036374; F:glutathione hydrolase activity; EXP:PomBase.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR GO; GO:0006751; P:glutathione catabolic process; ISM:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11686; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..419
FT /note="Glutathione hydrolase 2 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000247900"
FT CHAIN 420..611
FT /note="Glutathione hydrolase 2 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000247901"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..611
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 490..491
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 512..513
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 611 AA; 67825 MW; 5A74721D93CC8C26 CRC64;
MSPTDTTPLL YSWDDQSRHQ DPDWHKLRNY HGAWYRRISR RRFSQFIFAF GLMTLFVLVY
SISSNLHTPT QFTGHKVRGR RGAVASEVPV CSDIGVSMLA DGGNAVDAAI ASTFCIGVVN
FFSSGIGGGG FMLIKHPNET AQSLTFREIA PGNVSKHMFD KNPMLAQVGP LSIAIPGELA
GLYEAWKSHG LLDWSKLLEP NVKLAREGFP VTRAMERVLK LPEMAHLLKD PIWQPILMPN
GKVLRAGDKM FRPAYAKTLE IIANKGIEPF YRGELTNSMV KFIQDNGGIV TVEDFGNYST
VFADALHTSY RGHDVYTCTL PTSGPALIEG LNILDGYPLN TPSLAFPKRL HLEVEAMKWL
SAGRTQFGDP DFLPLDHLDV VSKLLSKEFA SQIRNNISLS KTYPWEHYNP SYDLPISHGT
THVSTVDSNN LAVSITSTVN LLFGSQLMDP VTGVVFNDQM DDFSIPGASN AFNLSPSPWN
FIEPFKRPQS SSAPTILTDI NGDFEMALGA SGGSRIVTAV LDSIIKRIDM DYDIESMVAS
ARPHHQLLPD ILILESGFSK SVATRMKKYG HKVWRLKQHD TPLSQIQAVT RHHSEYYGMS
DPRKYGQAAA Y
