ID Q2K8A6_RHIEC Unreviewed; 530 AA.
AC Q2K8A6;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=ggt1 {ECO:0000313|EMBL:ABC90930.1};
GN OrderedLocusNames=RHE_CH02146 {ECO:0000313|EMBL:ABC90930.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC90930.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC90930.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC90930.1; -; Genomic_DNA.
DR RefSeq; WP_011425412.1; NC_007761.1.
DR AlphaFoldDB; Q2K8A6; -.
DR MEROPS; T03.025; -.
DR KEGG; ret:RHE_CH02146; -.
DR eggNOG; COG0405; Bacteria.
DR HOGENOM; CLU_014813_3_2_5; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000001936; Chromosome.
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:ABC90930.1};
KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036};
KW Hydrolase {ECO:0000256|RuleBase:RU368036};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:ABC90930.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 530 AA; 56583 MW; F898C803D8B6E3CD CRC64;
MRNFELPGRS MAVGRNGMAA TSHPMATLTA IEILKAGGKA IDAAVGACAV QCVVEAGSTG
IGGDCFALLA SNGNDDVVAY NGSGRTPAAA HFAWFQENGI TSIERSSPHA VTVPGAVDAW
TRLVADHGRM PLSEILAPAI ALARDGYAIT PRVAADISNQ RDLLLRDPST RRLFLIDDQA
PLVGSVQHQP ELAQTLETIA TWGREGFYRG PVAADMVTRL NSLGGLHTVE DFALAAGEYV
KPVSATYRGW TVHECPPNGQ GIVALMILKI LERFERKGDP LGVDNLHIEV EATRLAYAAR
DRWVADMAAS DVPVDFLLSD ELADSLAARI DLNTIADAGA VVDGVEHADT VYISVVDKDR
NVASFINSIF HSYGSGVMAP NSGVLFHNRG QSFSLKQGHP NAIGPRKRPM HTIIPGLVTR
NGKSVLSFGV MGGHYQAMGH AHFLSKLFDF NLDIQSAIDL PRLFPLPGTT SIETEALLRS
SIGRDLEARG FKVVAPNWAI GGAQAIWIDD QNNTLLGASD HRKDGCALGY
//
