ID A0A2K2HA89_9BACT Unreviewed; 646 AA. AC A0A2K2HA89; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 27-NOV-2024, entry version 24. 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 Name=ggt {ECO:0000313|EMBL:PNU20216.1}; GN ORFNames=C2E25_08495 {ECO:0000313|EMBL:PNU20216.1}; OS Geothermobacter hydrogeniphilus. OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales; OC Geothermobacteraceae; Geothermobacter. OX NCBI_TaxID=1969733 {ECO:0000313|EMBL:PNU20216.1, ECO:0000313|Proteomes:UP000236340}; RN [1] {ECO:0000313|EMBL:PNU20216.1, ECO:0000313|Proteomes:UP000236340} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HR-1 {ECO:0000313|EMBL:PNU20216.1, RC ECO:0000313|Proteomes:UP000236340}; RA Smith H., Abuyen K., Tremblay J., Savalia P., Perez-Rodriguez I., RA Emerson D., Tully B., Amend J.; RT "Genome Sequence of Geothermobacter sp. HR-1 Iron Reducer from the Loihi RT Seamount."; RL Genome Announc. 0:0-0(2018). 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 N-terminal (5-L-glutamyl)-[peptide] + an alpha-amino acid = CC 5-L-glutamyl amino acid + an 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|ARBA:ARBA00009381, 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:PNU20216.1}. 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; PPFX01000016; PNU20216.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2K2HA89; -. DR UniPathway; UPA00204; -. DR Proteomes; UP000236340; Unassembled WGS sequence. DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule. 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; IPR051792; GGT-related_enzyme. DR InterPro; IPR043138; GGT_lsub_C. DR InterPro; IPR000101; GGT_peptidase. DR InterPro; IPR043137; GGT_ssub. DR InterPro; IPR029055; Ntn_hydrolases_N. DR NCBIfam; TIGR00066; g_glut_trans; 1. DR PANTHER; PTHR43199; GLUTATHIONE HYDROLASE; 1. DR PANTHER; PTHR43199:SF1; GLUTATHIONE HYDROLASE PROENZYME; 1. DR Pfam; PF01019; G_glu_transpept; 1. DR PRINTS; PR01210; GGTRANSPTASE. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, KW ECO:0000256|RuleBase:RU368036}; KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368036}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|RuleBase:RU368036}. FT REGION 56..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 56..71 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 462 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1" FT BINDING 187 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-2" FT BINDING 480..482 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-2" FT BINDING 504 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-2" FT BINDING 533..534 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-2" FT BINDING 555 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR600101-2" SQ SEQUENCE 646 AA; 68613 MW; 3A7AE37709C4220F CRC64; MMPPKRSWPA CMPSGGLPGF PTQPRCRTRR EVDMCRLCCL LLALGLSIAA CHAPQPLQPT SESSSPVQDE PSAAQVIPPG QVPPDERPPV VTPDISLEPL EKISPVAPSA PVFPVAAEEP FGVVAAVHPL AVAAGMRVLS GGGNAVDAAV AAALTLGVVD GYNSGIGGGC LILVRASGGE LLAIDGRETA PRLADREMFL HTGEADPDLS RNGPLAVGTP GTLAAYRLLL DKAGTKKLSD LIRPAADLAE QGFLIDGRYA DRLRRVAGRL KRDPGSAAIF LDRRGRPWPA GHRLRQPDLA ASYRSIAREG IAWFYRGAYA RSLDRWMRAH GGVLRFADLA DYRPVHRQPI RSGYRGLTIV GFPPPSSGGV LVAEILNILQ HFPLARLPAG PRLHLVAEAE KRAFADRAFW LGDADFVPVP RGLLDKGYAA ELAAGIDTEM ATPVPVAGTP PRAASDLFEH HTTHIAAADR AGNWVAITAT LNTSFGAKVV VPGSGIVLNN EMDDFAVAPG VPNSFGLVGA EANSVASGKR PLSSMSPTLV LQGKKPILTL GAAGGPTIIS QVVQVLINRF DLGMTLPAAV AAPRIHHQWR PDRLRVERRL SLPVRRVLEK AGHRLQTRGT IGVTQAVGRD REGHLRAVID PRLQAE //