GGT1_SCHPO
ID GGT1_SCHPO Reviewed; 630 AA.
AC Q9US04;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glutathione hydrolase proenzyme 1;
DE EC=3.4.19.13;
DE AltName: Full=Gamma-glutamyltransferase 1;
DE AltName: Full=Gamma-glutamyltranspeptidase 1;
DE EC=2.3.2.2;
DE Contains:
DE RecName: Full=Glutathione hydrolase 1 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 1 light chain;
DE Flags: Precursor;
GN Name=ggt1; ORFNames=SPAC664.09;
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], AND FUNCTION.
RX PubMed=15052323; DOI=10.1139/w03-106;
RA Park H.-J., Lim H.-W., Kim K., Kim I.-H., Park E.-H., Lim C.-J.;
RT "Characterization and regulation of the gamma-glutamyl transpeptidase gene
RT from the fission yeast Schizosaccharomyces pombe.";
RL Can. J. Microbiol. 50:61-66(2004).
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=15765057; DOI=10.1007/s12275-016-5562-5;
RA Kim H.-G., Park H.-J., Kang H.-J., Lim H.-W., Kim K., Park E.-H., Ahn K.,
RA Lim C.-J.;
RT "The Schizosaccharomyces pombe gene encoding gamma-glutamyl transpeptidase
RT I is regulated by non-fermentable carbon sources and nitrogen starvation.";
RL J. Microbiol. 43:44-48(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. {ECO:0000269|PubMed:15052323}.
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 -!- 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: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- INDUCTION: Induced upon nitrogen starvation. Also induced by non-
CC fermentable carbon sources such as glycerol, acetate and ethanol in a
CC pap1-independent manner. {ECO:0000269|PubMed:15765057}.
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; AF535133; AAN01227.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB65810.1; -; Genomic_DNA.
DR PIR; T50239; T50239.
DR RefSeq; NP_593457.1; NM_001018890.2.
DR AlphaFoldDB; Q9US04; -.
DR SMR; Q9US04; -.
DR BioGRID; 279953; 3.
DR STRING; 4896.SPAC664.09.1; -.
DR MEROPS; T03.011; -.
DR iPTMnet; Q9US04; -.
DR MaxQB; Q9US04; -.
DR PaxDb; Q9US04; -.
DR PRIDE; Q9US04; -.
DR EnsemblFungi; SPAC664.09.1; SPAC664.09.1:pep; SPAC664.09.
DR GeneID; 2543536; -.
DR KEGG; spo:SPAC664.09; -.
DR PomBase; SPAC664.09; ggt1.
DR VEuPathDB; FungiDB:SPAC664.09; -.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; Q9US04; -.
DR OMA; VCGMGPP; -.
DR PhylomeDB; Q9US04; -.
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:Q9US04; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
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: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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protease; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..440
FT /note="Glutathione hydrolase 1 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000247898"
FT CHAIN 441..630
FT /note="Glutathione hydrolase 1 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000247899"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..630
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 441
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 165
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 461
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 511..512
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 532..533
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 630 AA; 68722 MW; E85E83D21AC24B20 CRC64;
MGINTSSAQS SGAASIARSS VNVKSGNRHL SSNKKSATSA LEERASRPSI LVTFLVLAGT
ILSLYIWPIL SPDLFFANQR CSFKYKNKGS QRVVVEGKNG VVATEEETCS QIGVGILKAG
GNAVDAAIAS GICIGAVNSF SSGIGGGGFM LIRHPNGTAH SLNFRETAPA GASKNMFHGN
STLSQVGGLS VAVPGEIAGY ERAWKMYGSL PWHKLFEPTI RLMRDGMPMP KELASRIRRP
EFSYFKTHPD WSKIFAPEGV FLHVGEKFYR PALASTLEEI AKFGPEVFYT GKIAERLVKF
VQQQGGILTM EDMANFSVVV EEPIYGNFYD REVITCGSPC SGEALILGLN VLSKVDLSEG
TSILGCEMTD IGVHHLIETM KWMSAGRTVL ADPTFYNNTD HVEQLLSLEY ADEIRNNISN
ERTFDFTHYK AEYDFPNDHG TTHLSVIDKD NMAVGLTASI NLMFGSQLLE PETGIILNDH
MDDFASPGIV NAFGLSPSPY NFIAPGKRPQ SSAVPTILVY NGEVEMVLGG SGGSRIVTAV
LDTIIKKYKW GKSLLESVES PRFHHQLMPN IVYIDETVEI EVLRALEKFG HIVDLIPVQY
PFSEIQAVFR TNGTLYGLSD SRKQAVAAAY
