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Glutathione hydrolase proenzyme (EC 3.4.19.13) (CIK1 suppressor protein 2) (Extracellular mutant protein 38) (Gamma-glutamyltransferase) (EC 2.3.2.2) (Gamma-glutamyltranspeptidase) (Gamma-GT) [Cleaved into: Glutathione hydrolase heavy chain; Glutathione hydrolase light chain]

 ECM38_YEAST             Reviewed;         660 AA.
Q05902; D6VYU3;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 148.
RecName: Full=Glutathione hydrolase proenzyme;
EC=3.4.19.13 {ECO:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552};
AltName: Full=CIK1 suppressor protein 2;
AltName: Full=Extracellular mutant protein 38;
AltName: Full=Gamma-glutamyltransferase;
EC=2.3.2.2 {ECO:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552};
AltName: Full=Gamma-glutamyltranspeptidase;
Short=Gamma-GT;
Contains:
RecName: Full=Glutathione hydrolase heavy chain;
Contains:
RecName: Full=Glutathione hydrolase light chain;
Flags: Precursor;
Name=ECM38; Synonyms=CIS2; OrderedLocusNames=YLR299W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
CATALYTIC ACTIVITY, AND INDUCTION.
PubMed=6102906; DOI=10.1111/j.1432-1033.1980.tb04407.x;
Penninckx M., Jaspers C., Wiame J.M.;
"Glutathione metabolism in relation to the amino-acid permeation
systems of the yeast Saccharomyces cerevisiae. Occurrence of gamma-
glutamyltranspeptidase: its regulation and the effects of permeation
mutations on the enzyme cellular level.";
Eur. J. Biochem. 104:119-123(1980).
[4]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=6143552; DOI=10.1042/bj2180147;
Payne G.M., Payne J.W.;
"Gamma-glutamyltransferase is not involved in the bulk uptake of amino
acids, peptides or gamma-glutamyl-amino acids in yeast (Saccharomyces
cerevisiae).";
Biochem. J. 218:147-155(1984).
[5]
SUBCELLULAR LOCATION.
PubMed=6143574; DOI=10.1016/0300-9084(84)90193-7;
Jaspers C.J., Penninckx M.J.;
"Glutathione metabolism in yeast Saccharomyces cerevisiae. Evidence
that gamma-glutamyltranspeptidase is a vacuolar enzyme.";
Biochimie 66:71-74(1984).
[6]
ENZYME REGULATION.
PubMed=1674526; DOI=10.1099/00221287-137-3-637;
Elskens M.T., Jaspers C.J., Penninckx M.J.;
"Glutathione as an endogenous sulphur source in the yeast
Saccharomyces cerevisiae.";
J. Gen. Microbiol. 137:637-644(1991).
[7]
IDENTIFICATION.
PubMed=9335584;
Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J.,
Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W.,
Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.;
"Large scale identification of genes involved in cell surface
biosynthesis and architecture in Saccharomyces cerevisiae.";
Genetics 147:435-450(1997).
[8]
INDUCTION.
PubMed=9202464; DOI=10.1099/00221287-143-6-1885;
Mehdi K., Penninckx M.J.;
"An important role for glutathione and gamma-glutamyltranspeptidase in
the supply of growth requirements during nitrogen starvation of the
yeast Saccharomyces cerevisiae.";
Microbiology 143:1885-1889(1997).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11672438; DOI=10.1042/0264-6021:3590631;
Mehdi K., Thierie J., Penninckx M.J.;
"Gamma-glutamyl transpeptidase in the yeast Saccharomyces cerevisiae
and its role in the vacuolar transport and metabolism of
glutathione.";
Biochem. J. 359:631-637(2001).
[10]
INDUCTION.
PubMed=12529169; DOI=10.1042/BJ20021893;
Springael J.-Y., Penninckx M.J.;
"Nitrogen-source regulation of yeast gamma-glutamyl transpeptidase
synthesis involves the regulatory network including the GATA zinc-
finger factors Gln3, Nil1/Gat1 and Gzf3.";
Biochem. J. 371:589-595(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
VARIANTS ARG-171 AND ASP-494.
STRAIN=ATCC 76625 / YPH499;
PubMed=12868055; DOI=10.1002/yea.1012;
Kumar C., Sharma R., Bachhawat A.K.;
"Investigations into the polymorphisms at the ECM38 locus of two
widely used Saccharomyces cerevisiae S288C strains, YPH499 and
BY4742.";
Yeast 20:857-863(2003).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11672438}.
-!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
peptide + a 5-L-glutamyl amino acid. {ECO:0000269|PubMed:6102906,
ECO:0000269|PubMed:6143552}.
-!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
glutamate. {ECO:0000269|PubMed:6102906,
ECO:0000269|PubMed:6143552}.
-!- ENZYME REGULATION: Activity is decreased by glutathione and
ammonium ion. {ECO:0000269|PubMed:1674526}.
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- SUBUNIT: Heterodimer composed of a light and a heavy chain. The
active site is located in the light chain. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Vacuole membrane
{ECO:0000269|PubMed:11672438, ECO:0000269|PubMed:6143552,
ECO:0000269|PubMed:6143574}; Single-pass type II membrane protein
{ECO:0000269|PubMed:11672438, ECO:0000269|PubMed:6143552,
ECO:0000269|PubMed:6143574}.
-!- INDUCTION: 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.
{ECO:0000269|PubMed:12529169, ECO:0000269|PubMed:6102906,
ECO:0000269|PubMed:6143552, ECO:0000269|PubMed:9202464}.
-!- PTM: Cleaved by autocatalysis into a large and a small subunit.
-!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U17243; AAB67344.1; -; Genomic_DNA.
EMBL; BK006945; DAA09609.1; -; Genomic_DNA.
PIR; S50383; S50383.
RefSeq; NP_013402.1; NM_001182187.1.
ProteinModelPortal; Q05902; -.
SMR; Q05902; -.
BioGrid; 31563; 58.
DIP; DIP-4682N; -.
IntAct; Q05902; 3.
MINT; Q05902; -.
STRING; 4932.YLR299W; -.
MEROPS; T03.012; -.
MaxQB; Q05902; -.
PaxDb; Q05902; -.
PRIDE; Q05902; -.
EnsemblFungi; YLR299W; YLR299W; YLR299W.
GeneID; 851006; -.
KEGG; sce:YLR299W; -.
EuPathDB; FungiDB:YLR299W; -.
SGD; S000004290; ECM38.
GeneTree; ENSGT00550000074591; -.
HOGENOM; HOG000175620; -.
InParanoid; Q05902; -.
KO; K00681; -.
OMA; TKNMFLD; -.
OrthoDB; EOG092C24BM; -.
BioCyc; MetaCyc:YLR299W-MONOMER; -.
BioCyc; YEAST:YLR299W-MONOMER; -.
Reactome; R-SCE-174403; Glutathione synthesis and recycling.
Reactome; R-SCE-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-SCE-5423646; Aflatoxin activation and detoxification.
UniPathway; UPA00204; -.
PRO; PR:Q05902; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0036374; F:glutathione hydrolase activity; IMP:SGD.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0006751; P:glutathione catabolic process; IMP:SGD.
GO; GO:0006805; P:xenobiotic metabolic process; IMP:SGD.
InterPro; IPR000101; GGT_peptidase.
InterPro; IPR029055; Ntn_hydrolases_N.
PANTHER; PTHR11686; PTHR11686; 1.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR00066; g_glut_trans; 1.
PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Glycoprotein; Hydrolase; Membrane;
Protease; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix; Vacuole.
CHAIN 1 469 Glutathione hydrolase heavy chain.
{ECO:0000250}.
/FTId=PRO_0000011078.
CHAIN 470 660 Glutathione hydrolase light chain.
{ECO:0000250}.
/FTId=PRO_0000011079.
TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.
TRANSMEM 14 34 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 35 660 Lumenal. {ECO:0000255}.
REGION 540 541 Glutamate binding. {ECO:0000250}.
REGION 562 563 Glutamate binding. {ECO:0000250}.
ACT_SITE 470 470 Nucleophile. {ECO:0000250}.
BINDING 177 177 Glutamate. {ECO:0000250}.
BINDING 488 488 Glutamate. {ECO:0000250}.
BINDING 490 490 Glutamate. {ECO:0000250}.
BINDING 509 509 Glutamate. {ECO:0000250}.
BINDING 512 512 Glutamate. {ECO:0000250}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 454 454 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 517 517 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 171 171 H -> R (in strain: YPH499).
{ECO:0000269|PubMed:12868055}.
VARIANT 494 494 G -> D (in strain: YPH499; lack of gamma-
glutamyl transferase activity).
{ECO:0000269|PubMed:12868055}.
SEQUENCE 660 AA; 73180 MW; 9896E9EBFF822F55 CRC64;
MLLCNRKVPK TLNTCFILHI FTLLTLGVLV SGMPSKMVSF ASQETLQRIN NLLRGSANRD
VDIIAEYLKK DDDDDGGDKD HHNIDIDPLP RRPSLTPDRQ LLKVGLHGAI SSDLEVCSNL
TINEVLLKFP GSNAADAAVT QALCKGMVNF FNSGIGGGGY VVFSGKDDED HLSIDFREKA
PMDSHKFMFE NCSLCSKIGG LAVGVPGELM GLYRLFKERG SGQVDWRDLI EPVAKLGSVG
WQIGEALGAT LELYEDVFLT LKEDWSFVLN STHDGVLKEG DWIKRPALSN MLMELAKNGS
VAPFYDPDHW IAKSMIDTVA KYNGIMNLQD VSSYDVHVTK PLSMKIRKGA NFIPDNDMTV
LTSSGSSSGA ALLAALRIMD NFQNQEGGDY EKETTYHLLE SMKWMASARS RLGDFEGEAL
PKHIEEVLDP EWALKAVKSI KRNSQDGNFK TLENWTLYDP AYDINNPHGT AHFSIVDSHG
NAVSLTTTIN LLFGSLVHDP KTGVIFNNEM DDFAQFNKSN SFELAPSIYN FPEPGKRPLS
STAPTIVLSE LGIPDLVVGA SGGSRITTSV LQTIVRTYWY NMPILETIAY PRIHHQLLPD
RIELESFPMI GKAVLSTLKE MGYTMKEVFP KSVVNAIRNV RGEWHAVSDY WRKRGISSVY


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