ID ECM38_YEAST Reviewed; 660 AA. AC Q05902; D6VYU3; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 08-JUN-2016, entry version 131. DE RecName: Full=Gamma-glutamyltransferase; DE EC=2.3.2.2 {ECO:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552}; DE AltName: Full=CIK1 suppressor protein 2; DE AltName: Full=Extracellular mutant protein 38; DE AltName: Full=Gamma-glutamyltranspeptidase; DE Short=Gamma-GT; DE AltName: Full=Glutathione hydrolase; DE EC=3.4.19.13 {ECO:0000269|PubMed:6102906, ECO:0000269|PubMed:6143552}; DE Contains: DE RecName: Full=Gamma-glutamyltransferase heavy chain; DE Contains: DE RecName: Full=Gamma-glutamyltransferase light chain; DE Flags: Precursor; GN Name=ECM38; Synonyms=CIS2; OrderedLocusNames=YLR299W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP CATALYTIC ACTIVITY, AND INDUCTION. RX PubMed=6102906; DOI=10.1111/j.1432-1033.1980.tb04407.x; RA Penninckx M., Jaspers C., Wiame J.M.; RT "Glutathione metabolism in relation to the amino-acid permeation RT systems of the yeast Saccharomyces cerevisiae. Occurrence of gamma- RT glutamyltranspeptidase: its regulation and the effects of permeation RT mutations on the enzyme cellular level."; RL Eur. J. Biochem. 104:119-123(1980). RN [4] RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=6143552; RA Payne G.M., Payne J.W.; RT "Gamma-glutamyltransferase is not involved in the bulk uptake of amino RT acids, peptides or gamma-glutamyl-amino acids in yeast (Saccharomyces RT cerevisiae)."; RL Biochem. J. 218:147-155(1984). RN [5] RP SUBCELLULAR LOCATION. RX PubMed=6143574; DOI=10.1016/0300-9084(84)90193-7; RA Jaspers C.J., Penninckx M.J.; RT "Glutathione metabolism in yeast Saccharomyces cerevisiae. Evidence RT that gamma-glutamyltranspeptidase is a vacuolar enzyme."; RL Biochimie 66:71-74(1984). RN [6] RP ENZYME REGULATION. RX PubMed=1674526; RA Elskens M.T., Jaspers C.J., Penninckx M.J.; RT "Glutathione as an endogenous sulphur source in the yeast RT Saccharomyces cerevisiae."; RL J. Gen. Microbiol. 137:637-644(1991). RN [7] RP IDENTIFICATION. RX PubMed=9335584; RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., RA Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., RA Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.; RT "Large scale identification of genes involved in cell surface RT biosynthesis and architecture in Saccharomyces cerevisiae."; RL Genetics 147:435-450(1997). RN [8] RP INDUCTION. RX PubMed=9202464; RA Mehdi K., Penninckx M.J.; RT "An important role for glutathione and gamma-glutamyltranspeptidase in RT the supply of growth requirements during nitrogen starvation of the RT yeast Saccharomyces cerevisiae."; RL Microbiology 143:1885-1889(1997). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11672438; DOI=10.1042/0264-6021:3590631; RA Mehdi K., Thierie J., Penninckx M.J.; RT "Gamma-glutamyl transpeptidase in the yeast Saccharomyces cerevisiae RT and its role in the vacuolar transport and metabolism of RT glutathione."; RL Biochem. J. 359:631-637(2001). RN [10] RP INDUCTION. RX PubMed=12529169; DOI=10.1042/BJ20021893; RA Springael J.-Y., Penninckx M.J.; RT "Nitrogen-source regulation of yeast gamma-glutamyl transpeptidase RT synthesis involves the regulatory network including the GATA zinc- RT finger factors Gln3, Nil1/Gat1 and Gzf3."; RL Biochem. J. 371:589-595(2003). RN [11] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [12] RP VARIANTS ARG-171 AND ASP-494. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=12868055; DOI=10.1002/yea.1012; RA Kumar C., Sharma R., Bachhawat A.K.; RT "Investigations into the polymorphisms at the ECM38 locus of two RT widely used Saccharomyces cerevisiae S288C strains, YPH499 and RT BY4742."; RL Yeast 20:857-863(2003). CC -!- FUNCTION: Catalyzes the transfer of the gamma-glutamyl moiety of CC glutathione (GSH) and other gamma-glutamyl compounds to amino CC acids and peptides. Major GSH-degrading enzyme, catalyzing the CC hydrolytic release of L-glutamate from GSH. Plays a role in the CC turnover of the vacuolar GSH, serving as an alternative nitrogen CC source during nitrogen starvation. {ECO:0000269|PubMed:11672438}. CC -!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a CC peptide + a 5-L-glutamyl amino acid. {ECO:0000269|PubMed:6102906, CC ECO:0000269|PubMed:6143552}. CC -!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L- CC glutamate. {ECO:0000269|PubMed:6102906, CC ECO:0000269|PubMed:6143552}. CC -!- ENZYME REGULATION: Activity is decreased by glutathione and CC ammonium ion. {ECO:0000269|PubMed:1674526}. CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism. CC -!- SUBUNIT: Heterodimer composed of a light and a heavy chain. The CC active site is located in the light chain. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Vacuole membrane CC {ECO:0000269|PubMed:11672438, ECO:0000269|PubMed:6143552, CC ECO:0000269|PubMed:6143574}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:11672438, ECO:0000269|PubMed:6143552, CC ECO:0000269|PubMed:6143574}. CC -!- INDUCTION: Induced upon nitrogen starvation. Repressed by ammonium CC ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible CC inhibitors whereas serine-borate is a reversible inhibitor. CC {ECO:0000269|PubMed:12529169, ECO:0000269|PubMed:6102906, CC ECO:0000269|PubMed:6143552, ECO:0000269|PubMed:9202464}. CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit. CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U17243; AAB67344.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09609.1; -; Genomic_DNA. DR PIR; S50383; S50383. DR RefSeq; NP_013402.1; NM_001182187.1. DR ProteinModelPortal; Q05902; -. DR SMR; Q05902; 102-638. DR BioGrid; 31563; 19. DR DIP; DIP-4682N; -. DR MINT; MINT-481929; -. DR MEROPS; T03.012; -. DR MaxQB; Q05902; -. DR EnsemblFungi; YLR299W; YLR299W; YLR299W. DR GeneID; 851006; -. DR KEGG; sce:YLR299W; -. DR EuPathDB; FungiDB:YLR299W; -. DR SGD; S000004290; ECM38. DR GeneTree; ENSGT00550000074591; -. DR HOGENOM; HOG000175620; -. DR InParanoid; Q05902; -. DR KO; K00681; -. DR OMA; DRAADFK; -. DR OrthoDB; EOG7BCNMD; -. DR BioCyc; YEAST:YLR299W-MONOMER; -. DR Reactome; R-SCE-174403; Glutathione synthesis and recycling. DR Reactome; R-SCE-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX). DR Reactome; R-SCE-5423646; Aflatoxin activation and detoxification. DR UniPathway; UPA00204; -. DR PRO; PR:Q05902; -. DR Proteomes; UP000002311; Chromosome XII. DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003840; F:gamma-glutamyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0036374; F:glutathione hydrolase activity; IMP:SGD. DR GO; GO:0006751; P:glutathione catabolic process; IMP:SGD. DR GO; GO:0006805; P:xenobiotic metabolic process; IMP:SGD. DR InterPro; IPR000101; GGT_peptidase. DR InterPro; IPR029055; Ntn_hydrolases_N. DR PANTHER; PTHR11686; PTHR11686; 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR00066; g_glut_trans; 1. DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1. PE 1: Evidence at protein level; KW Acyltransferase; Complete proteome; Glycoprotein; Hydrolase; Membrane; KW Protease; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix; Vacuole. FT CHAIN 1 469 Gamma-glutamyltransferase heavy chain. FT {ECO:0000250}. FT /FTId=PRO_0000011078. FT CHAIN 470 660 Gamma-glutamyltransferase light chain. FT {ECO:0000250}. FT /FTId=PRO_0000011079. FT TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 14 34 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 35 660 Lumenal. {ECO:0000255}. FT REGION 540 541 Glutamate binding. {ECO:0000250}. FT REGION 562 563 Glutamate binding. {ECO:0000250}. FT ACT_SITE 470 470 Nucleophile. {ECO:0000250}. FT BINDING 177 177 Glutamate. {ECO:0000250}. FT BINDING 488 488 Glutamate. {ECO:0000250}. FT BINDING 490 490 Glutamate. {ECO:0000250}. FT BINDING 509 509 Glutamate. {ECO:0000250}. FT BINDING 512 512 Glutamate. {ECO:0000250}. FT CARBOHYD 119 119 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 191 191 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 270 270 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 298 298 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 454 454 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 517 517 N-linked (GlcNAc...). {ECO:0000255}. FT VARIANT 171 171 H -> R (in strain: YPH499). FT {ECO:0000269|PubMed:12868055}. FT VARIANT 494 494 G -> D (in strain: YPH499; lack of gamma- FT glutamyl transferase activity). FT {ECO:0000269|PubMed:12868055}. SQ 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 //