ID A0A1E3UVJ4_9GAMM Unreviewed; 570 AA. AC A0A1E3UVJ4; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 22-FEB-2023, entry version 16. DE RecName: Full=Glutathione hydrolase proenzyme {ECO:0000256|RuleBase:RU368036}; DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368036}; DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368036}; DE Contains: DE RecName: Full=Glutathione hydrolase large chain {ECO:0000256|RuleBase:RU368036}; DE Contains: DE RecName: Full=Glutathione hydrolase small chain {ECO:0000256|RuleBase:RU368036}; GN ORFNames=ABT47_04390 {ECO:0000313|EMBL:ODR84606.1}; OS Shewanella xiamenensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=332186 {ECO:0000313|EMBL:ODR84606.1, ECO:0000313|Proteomes:UP000094602}; RN [1] {ECO:0000313|EMBL:ODR84606.1, ECO:0000313|Proteomes:UP000094602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T17 {ECO:0000313|EMBL:ODR84606.1, RC ECO:0000313|Proteomes:UP000094602}; RA Yousfi K., Touati A., Lefebvre B., Fournier E., Walker M., Reimer A., RA Bougdour D., Bekal S.; RT "Identification of antibiotic resistance genes in Shewanella xiamenensis."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. 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:RU368036}; 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:RU368036}; 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:RU368036}; CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism. CC {ECO:0000256|RuleBase:RU368036}. CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are CC synthesized in precursor form from a single polypeptide. CC {ECO:0000256|RuleBase:RU368036}. CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit. CC {ECO:0000256|RuleBase:RU368036}. CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family. CC {ECO:0000256|RuleBase:RU368036}. 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:ODR84606.1}. 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; LDOA01000001; ODR84606.1; -; Genomic_DNA. DR RefSeq; WP_069453567.1; NZ_LVDQ01000017.1. DR AlphaFoldDB; A0A1E3UVJ4; -. DR STRING; 332186.ABT47_04390; -. DR EnsemblBacteria; ODR84606; ODR84606; ABT47_04390. DR PATRIC; fig|332186.8.peg.917; -. DR OrthoDB; 5297205at2; -. DR UniPathway; UPA00204; -. DR Proteomes; UP000094602; 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:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW. 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; PTHR43881; GAMMA-GLUTAMYLTRANSPEPTIDASE (AFU_ORTHOLOGUE AFUA_4G13580); 1. DR PANTHER; PTHR43881:SF1; GAMMA-GLUTAMYLTRANSPEPTIDASE (AFU_ORTHOLOGUE AFUA_4G13580); 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 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU368036}; KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036}; KW Hydrolase {ECO:0000256|RuleBase:RU368036}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:ODR84606.1}; KW Zymogen {ECO:0000256|RuleBase:RU368036}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..570 FT /note="Glutathione hydrolase proenzyme" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5009137591" SQ SEQUENCE 570 AA; 61614 MW; E0A7F207B55189A8 CRC64; MIKTIKSICT LVTVATAMSS SGVLAMDRIT GKAFATRSEV YATHGMAATS QPLATQVAID VLKQGGSAVD AAIAANAMLG LVEPTGSGVG GDLFAIVWSA KDKKLYGLNA SGRSPKSLTL EKLKSLGLDY LPPLGPLPVS VPGAVDGWFE LHDKFGKLPM ADNLAPAIRY AREGFPVSEL IAYYLEGSGK KLAQFPGFKE TYMPNGKMPA VGEIFKNPAL ANTYEKIAKG GRDAFYKGDI AKSIDKYIKA QGGYLSYEDL ASHTSDWIEP VSVNYRGYDV WELPPNGQGI AALQILKTME PFDVATMGFN SPEYVHLFVE AKKLAFADRA KFYADMAFNK VPVKELISQQ YNYDRAKLID LNKAAKSVDA GNPALQHGDT VYLTTADKDG NMVSLIQSNY RGMGSGMTPP DLGFVLQDRG QMFDLTEGRF NTYAPGKRPF HTIIPAFVTK DGKPWLSFGV MGGATQPQMH AQIIINLIDF KMNLQEAGDA PRILHSGSTE PTGEIMNDGG YVSLESGFPV ETRRELMKKG HVLRDVLGDF GGYQAIGFNA ETGVYRGASE SRKDGYAAGY //