ID B5JXQ4_9GAMM Unreviewed; 570 AA.
AC B5JXQ4;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:EDY85588.1};
GN ORFNames=GP5015_469 {ECO:0000313|EMBL:EDY85588.1};
OS gamma proteobacterium HTCC5015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY85588.1, ECO:0000313|Proteomes:UP000004692};
RN [1] {ECO:0000313|Proteomes:UP000004692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX PubMed=20472792; DOI=10.1128/JB.00510-10;
RA Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequence of the novel marine member of the Gammaproteobacteria
RT strain HTCC5015.";
RL J. Bacteriol. 192:3838-3839(2010).
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}.
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DR EMBL; DS990613; EDY85588.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JXQ4; -.
DR STRING; 391615.GP5015_469; -.
DR MEROPS; T03.001; -.
DR eggNOG; COG0405; Bacteria.
DR HOGENOM; CLU_014813_0_3_6; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000004692; 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; PTHR43199; GLUTATHIONE HYDROLASE; 1.
DR PANTHER; PTHR43199:SF6; 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|RuleBase:RU368036};
KW Reference proteome {ECO:0000313|Proteomes:UP000004692};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:EDY85588.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..570
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002836045"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 570 AA; 60373 MW; 9550AC0FECC70FBC CRC64;
MWQNIVVGAA LLASSVVGAA QSGAQLALPQ QAAVASAHPK ATEAGHRVLA QGGNACDAAV
AVTAALAVVE PYGSGLGGGG FYLTRTAEGK AKMLDARETA PADASADMYL DSHGDVVPRL
SIDGPLAAGI PGIPAALDEL SSRCGQLSLA DSLAPAIELA EQGFAFDQKI VDMLGFRQQA
IAASPAASEI FFNNGELPKV GEVLVQRDLA AVLKRIAERG REGFYAGDTA EALVEGVQRA
GGIWQLKDLD NYRPQWREPV VGEYRGMSVT AAGLPSSGGI VLLQMLNILR QFPEDSLEMD
RPLALHLQVE AMRRAYRDRA EYLGDADFVD VPRERLLSPH YAAGLAASIR SDRATPSESL
PGIVQAAGGE DTTHFSIVDR QGNAVAATLS INYPFGSGFV PPGTGVLLND EMDDFSSKPG
VANVYGLVGS RANAIAPNKR MLSSMTPTFI EKDNKLLALG SPGGSRIITM VLRGALDFYR
GRTLNDIVSA PRIHHQFLPD VVQFEPEALS RNQQLELQLM GHELKEMGRQ YGNMQAVLWD
MASGEVEAAS DPRGLGRADL GSYGENTASQ
//
