ID A0A2A2II06_9BACI Unreviewed; 537 AA.
AC A0A2A2II06;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:PAV30936.1};
GN ORFNames=CIL05_04265 {ECO:0000313|EMBL:PAV30936.1};
OS Virgibacillus profundi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=2024555 {ECO:0000313|EMBL:PAV30936.1, ECO:0000313|Proteomes:UP000218887};
RN [1] {ECO:0000313|EMBL:PAV30936.1, ECO:0000313|Proteomes:UP000218887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IO3-P3-H5 {ECO:0000313|EMBL:PAV30936.1,
RC ECO:0000313|Proteomes:UP000218887};
RA Xu B., Hu B., Wang J., Zhu Y., Huang L., Du W., Huang Y.;
RT "Virgibacillus indicus sp. nov. and Virgibacillus profoundi sp. nov, two
RT moderately halophilic bacteria isolated from marine sediment by using the
RT Microfluidic Streak Plate.";
RL Submitted (AUG-2017) 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:PAV30936.1}.
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DR EMBL; NPOA01000002; PAV30936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2II06; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000218887; 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; 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; 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.
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:PAV30936.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 537 AA; 58321 MW; 42A8AAD82104BF11 CRC64;
MMSFNNQSSP YPVTRNATYA KKGMVATSQP LASQAGLDIL KKGGNAIDAA IATAACLTVV
EPTSNGIGGD AFALVWTKDK LHGLNASGRS PKNISIEAVK KAGYEEIPAH GWIPVTVPGA
PGAWAELSKK FGKLPLTEVL EPAITYASEG FPVSPTLSKY WKKGYNSFKK HLTDDVYENW
FKTFAPNDRA PKAGEIWSSP DHAKTLQSIA ETNGESFYRG ELAEKIAAFS KENGGFLTAE
DLAEHKTDWV DPISVNYRGY DVWEIPPNGQ GIVALQALNI LKGFEFTEKE SVETYHKQIE
AIKLAFADGQ AHVTEEGNMK YRSDDILSDV YAETRRKLIS EEALQPEAGE PTGSGTVYLA
TADSEGNMVS FIQSNYMGFG SGLVVPGTGI ALQNRGHNFS MDSGHVNALA GGKRTYHTII
PGFLTKDNQP VGPFGVMGGF MQPQGHLQVV MNTIDFGLNP QAALDAPRWQ WMKEKTVEVE
NRFGHHLAQG LADRGHDIQI QLEPNSFGRG QIIWRDPETG VLAGGTESRT DGTVAPW
//
