ID A0A0R0BYB2_9GAMM Unreviewed; 582 AA.
AC A0A0R0BYB2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=ABB25_06420 {ECO:0000313|EMBL:KRG58289.1};
OS Stenotrophomonas koreensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=266128 {ECO:0000313|EMBL:KRG58289.1, ECO:0000313|Proteomes:UP000051254};
RN [1] {ECO:0000313|EMBL:KRG58289.1, ECO:0000313|Proteomes:UP000051254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17805 {ECO:0000313|EMBL:KRG58289.1,
RC ECO:0000313|Proteomes:UP000051254};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
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:KRG58289.1}.
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DR EMBL; LDJH01000011; KRG58289.1; -; Genomic_DNA.
DR RefSeq; WP_057665095.1; NZ_LDJH01000011.1.
DR AlphaFoldDB; A0A0R0BYB2; -.
DR STRING; 266128.ABB25_06420; -.
DR PATRIC; fig|266128.3.peg.149; -.
DR OrthoDB; 5297205at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000051254; 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 Reference proteome {ECO:0000313|Proteomes:UP000051254};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:KRG58289.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..582
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006393217"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 582 AA; 62963 MW; 67EF8530294DB409 CRC64;
MRRLPSSCRH LRPLLLAGAL LCAVLPAAAA DRISGQAFAT RSEVIAPQAM AATSHPLATQ
IALDMLKAGG SAMDAAIAAN AALGLMEPTG NGIGGDLFAI VWDPKTQKLH GYNGSGRSPR
ALTVEEFHRR GLSEIPAHGP LPVSVPGTVD AWFALHERFG KRPMADNLAP TIAYARNGHP
VHEVIAHYWE RSVPRLSPYP GFVEQFTIDG RAPRKGQMWR NPNLANTLEA IARGGRDAFY
KGDIARTMDA YFRRHDGFLR YEDLASHQGE WVEPVSSNYR GHDVWELPPN SQGIAALQIL
NILEGYDFSK IPFGSAEHVH LFTEAKKIAF ADRARFYADP AFSPAPVAQL ISKGYAAARR
AGIDPQRAAR VVQPATPAQL EEGDTIYLTT ADADGMMVSL IQSNYRGMGS GMAPDGLGFI
LQDRGEMFVL PPPGQTSDHP NAYAPGKRPF QTIIPAFITK DGKPWVSFGV MGGAMQPQGH
AQIVMNLIDF GMNLQEAGDA PRIQHERSTE PTGQATAMSD GGEINLETGF PYATVRALMQ
MGHKVTFADG PYGGYQAIMR DHEQGVYIGA SESRKDGQAA GY
//
