ID A0A1E3L7S5_9BACL Unreviewed; 529 AA.
AC A0A1E3L7S5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=PTI45_00907 {ECO:0000313|EMBL:ODP29753.1};
OS Paenibacillus nuruki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP29753.1, ECO:0000313|Proteomes:UP000094578};
RN [1] {ECO:0000313|EMBL:ODP29753.1, ECO:0000313|Proteomes:UP000094578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP29753.1,
RC ECO:0000313|Proteomes:UP000094578};
RA Kim S.-J.;
RT "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT traditional nuruk.";
RL Submitted (AUG-2016) 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:ODP29753.1}.
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DR EMBL; MDER01000029; ODP29753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3L7S5; -.
DR STRING; 1886670.PTI45_00907; -.
DR PATRIC; fig|1886670.3.peg.928; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000094578; 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 ECO:0000313|EMBL:ODP29753.1};
KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036};
KW Hydrolase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:ODP29753.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094578};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:ODP29753.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 529 AA; 58469 MW; 30E5F530CEB9D93A CRC64;
MNIMPQSRRG MVAAPHYLAS QTGAFILQSG GNAFDAAVAV SAVLGVVYPH MTGPGGDAFF
LIHDGRTGKI EGYNGSGRSA SKATPEWYTK QGYTSIPSRG PLAAVTVPGM VDAWENVWKK
YGRLSWAEIM APAVRYAEEG FPASPSLARW IIRDLEWIQQ DSHLQSVFCP QGIPLVEGDI
VVQHKLAQTL RLISEQGSEC FYRGSIGQMI GEATERDGSV LTTADLAAHQ GEWVEPVSTT
YRGHEVYQMP PNTQGFSVLM MLNILENVEL SSIARFSPEF YHLVVETVKK AFQDRDRYLT
DPAFREIPLE QLLSKDYARK LWYDMQYRPQ ASPHLSPAMG QDTAYAAVTD DEGNTVSFIQ
SLYFDFGSAY VPGDSGVILQ NRGSFFSLDD RAPNVLEPRK RTFHTLMPGM VTKNGKPYLL
LGTQGGEGQP QTQLSILTGV IDYQLNIQQA IGLPRWLYGR TWGDMSDTLK IESRSYEDIY
SRLEAYGHIV EPIRDYDAVM GEAQGIMISE QGVFSGAADP RSDGIAIGI
//
