ID A0A1P8JRL1_9BURK Unreviewed; 528 AA.
AC A0A1P8JRL1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=RD110_03490 {ECO:0000313|EMBL:APW36380.1}, RD110_26820
GN {ECO:0000313|EMBL:APW41000.1};
OS Rhodoferax koreense.
OG Plasmid unnamed1 {ECO:0000313|EMBL:APW41000.1}, and
OG Plasmid unnamed1 sequence {ECO:0000313|Proteomes:UP000186609}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1842727 {ECO:0000313|EMBL:APW36380.1, ECO:0000313|Proteomes:UP000186609};
RN [1] {ECO:0000313|EMBL:APW36380.1, ECO:0000313|Proteomes:UP000186609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY110 {ECO:0000313|EMBL:APW36380.1,
RC ECO:0000313|Proteomes:UP000186609};
RC PLASMID=Plasmid unnamed1 sequence {ECO:0000313|Proteomes:UP000186609},
RC and unnamed1 {ECO:0000313|EMBL:APW41000.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; CP019236; APW36380.1; -; Genomic_DNA.
DR EMBL; CP019237; APW41000.1; -; Genomic_DNA.
DR RefSeq; WP_076196734.1; NZ_CP019237.1.
DR AlphaFoldDB; A0A1P8JRL1; -.
DR STRING; 1842727.RD110_03490; -.
DR KEGG; rhy:RD110_03490; -.
DR KEGG; rhy:RD110_26820; -.
DR OrthoDB; 5297205at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000186609; Chromosome.
DR Proteomes; UP000186609; Plasmid unnamed1 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 Plasmid {ECO:0000313|EMBL:APW41000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186609};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:APW36380.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 528 AA; 56329 MW; 235FCA5B33E113E6 CRC64;
MRDFEAPSRS VAVGSRGMVA TSNPQAALAG LDVLRSGGNA IDAAVAAAAM LAVVEPTQTG
IGGDCFVMLR KRGQAPVALN GSGWAAKAAS AEELRGRGMA SIPVDSVHAL TVPGAVRAWN
RLVEDYGTRS LQELLEPAIG AAELGYLVTE RLAHDWARQA AKMMATAEAK ALFFPAGRAP
ALGERRSNPQ LGKTLRAIAK SGADSFYEGW VAENIVTSLR KKGSLLSLDD FAEFKPEYVT
PISASYRGYR LWECPPNGQG VVALQIAAML EAFDLSAMGP LSAERFHLQA ELSRIAYAQR
NAFLCDPRFN AVDVNELLSD DTIERLTRGI DLDTKSDGWT PVALPEHKDT VYVSVADSDG
TLVSFINSIY DDFGSGIVAP GTGVLMHNRG SGFVLEEGHP NELQGRKRPM HTIIPALVTK
DADTVMSFGV TGGHFQPAGQ LQVLSNIVDY GMSVQQAIDH ARMFARGDVL ELERTVPDAV
WSGLRKRGHE PVAAPSPLGT CHAIWVDQGS GVYMGGSDGR RDGLAIGF
//
