ID E9ERN9_METRA Unreviewed; 572 AA. AC E9ERN9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 2. DT 22-FEB-2023, entry version 46. DE RecName: Full=Glutathione hydrolase {ECO:0000256|RuleBase:RU368068}; DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368068}; DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368068}; DE AltName: Full=Gamma-glutamyltransferase {ECO:0000256|RuleBase:RU368068}; DE AltName: Full=Gamma-glutamyltranspeptidase {ECO:0000256|RuleBase:RU368068}; GN ORFNames=MAA_02635 {ECO:0000313|EMBL:EFZ01406.2}; OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium OS anisopliae (strain ARSEF 23)). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium. OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ01406.2, ECO:0000313|Proteomes:UP000002498}; RN [1] {ECO:0000313|EMBL:EFZ01406.2, ECO:0000313|Proteomes:UP000002498} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498}; RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264; RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X., RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S., RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y., RA Wang C.; RT "Genome sequencing and comparative transcriptomics of the model RT entomopathogenic fungi Metarhizium anisopliae and M. acridum."; RL PLoS Genet. 7:E1001264-E1001264(2011). RN [2] {ECO:0000313|EMBL:EFZ01406.2, ECO:0000313|Proteomes:UP000002498} RP GENOME REANNOTATION. RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498}; RX PubMed=25368161; DOI=10.1073/pnas.1412662111; RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S., RA St Leger R.J., Wang C.; RT "Trajectory and genomic determinants of fungal-pathogen speciation and host RT adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014). CC -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and CC glutathione conjugates. {ECO:0000256|RuleBase:RU368068}. 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 Evidence={ECO:0000256|ARBA:ARBA00001049, CC ECO:0000256|RuleBase:RU368068}; 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:0000256|ARBA:ARBA00000250, CC ECO:0000256|RuleBase:RU368068}; 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 Evidence={ECO:0000256|ARBA:ARBA00001089, CC ECO:0000256|RuleBase:RU368068}; CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism. CC {ECO:0000256|RuleBase:RU368068}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EFZ01406.2}. 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; ADNJ02000004; EFZ01406.2; -; Genomic_DNA. DR RefSeq; XP_007818824.2; XM_007820633.2. DR AlphaFoldDB; E9ERN9; -. DR MEROPS; T03.011; -. DR GeneID; 19256921; -. DR KEGG; maj:MAA_02635; -. DR HOGENOM; CLU_014813_4_0_1; -. DR OrthoDB; 2910309at2759; -. DR UniPathway; UPA00204; -. DR Proteomes; UP000002498; Unassembled WGS sequence. DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule. 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:0006751; P:glutathione catabolic process; IEA:UniProtKB-UniRule. 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; GAMMA GLUTAMYL TRANSPEPTIDASE; 1. DR PANTHER; PTHR11686:SF62; GAMMA-GLUTAMYLTRANSPEPTIDASE (EUROFUNG); 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR TIGRFAMs; TIGR00066; g_glut_trans; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000256|RuleBase:RU368068}; KW Hydrolase {ECO:0000256|RuleBase:RU368068}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|RuleBase:RU368068}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..572 FT /note="Glutathione hydrolase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003238778" SQ SEQUENCE 572 AA; 61740 MW; 2D1A71B28287F2BF CRC64; MVETLMPHLA RLLLASLANY GFTHASALPE VVFRPTTDGS LGAVASESAE CSAIGRDLLA RGGNAADALV GTTFCVGVIG MYHSGIGGGG FAIVRDSAGN YEAVDFREAA PAAGHEDMYQ GNVPGSIYGG LAVGVPSEVL GLEYIHSKYG SLPWKTVMQG AIHVARHGFR VSNDLVGYIE RAVKEKPNFL VEDPNWAQDF APNGSLLQVG EIMTRKRYAN TLEKIANQGS KVFYTGELAE TLVNYIQQTN GTLTLSDFKN YKVISRPVKN VTYRGLHLYT IGTPASGSIT LNILKIMEQF DEADSKDTNL TSHRFVEAMR FGYGARAELG DPAFVEGLDE YEAHLLDDVH AKQIRERISD KQTLPVREYN PKGVALPESH GTSHIVTADR SGMATSLTTT VNLLFGAQIM DPSSGIILNN EMNDFSIPGV PNEFGFQPSV ANFIRPGKRP LSSVTPVIAA FPDGKLFATV GAAGGSRIIS STTSALWHTI EQEMTMKEAL REPRLHDQVM PNTLLLEYGF DAETAAGLGE RKHNITWVGP GLSAVQGIRR LRDGSFEAAS EPRQKNSGGF TI //