ID   A0A2K2HA89_9DELT        Unreviewed;       646 AA.
AC   A0A2K2HA89;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   19-JAN-2022, entry version 14.
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; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; 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 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:PNU20216.1}.
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DR   EMBL; PPFX01000016; PNU20216.1; -; Genomic_DNA.
DR   EnsemblBacteria; PNU20216; PNU20216; C2E25_08495.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000236340; 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   SUPFAM; SSF56235; SSF56235; 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   Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:PNU20216.1};
KW   Zymogen {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"
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
//