ID A0A1E3LRL0_9SPHN Unreviewed; 572 AA.
AC A0A1E3LRL0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BFL28_06405 {ECO:0000313|EMBL:ODP36386.1};
OS Sphingomonas turrisvirgatae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1888892 {ECO:0000313|EMBL:ODP36386.1, ECO:0000313|Proteomes:UP000094487};
RN [1] {ECO:0000313|EMBL:ODP36386.1, ECO:0000313|Proteomes:UP000094487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCT13 {ECO:0000313|EMBL:ODP36386.1,
RC ECO:0000313|Proteomes:UP000094487};
RA D'Andrea M.M., Rossolini G.M., Thaller M.C.;
RT "Draft genome of the agarase producing Sphingomonas sp. MCT13.";
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|ARBA:ARBA00009381, 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:ODP36386.1}.
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DR EMBL; MDDS01000075; ODP36386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3LRL0; -.
DR STRING; 1888892.BFL28_06405; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000094487; 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:SF1; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368036};
KW Reference proteome {ECO:0000313|Proteomes:UP000094487};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..572
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009131905"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 572 AA; 61076 MW; A0A5491F411C6E71 CRC64;
MMFRKFTLAL SALALALPMP VAAQSRHLLE YPSIHSPTVG TRGMVVSQNA IASDVGAQIL
RAGGNAVDAA VAVGFALAVT LPRAGNIGGD GFMTVYDAKS KQVRVLDFRG IAPRAATPAM
FVDEKGEERG IASYGYLAPA VPGTVAGLEQ AHRKWGKLPW AKLVEPAIRL ARDGVKLTAD
EAFVFGWGRQ RLARSASGKA VFYKPDGSLY AKDELLRQPD LAWTLEQIAK GGAKAFYTGE
IARRIEADMK ANGGLITRAD LASYAPVERD PLVGTYRGLQ VYTTPPASAG GATLINMLNM
LEHFDLKGMG AGSAASLHVM AEAMKLAYLD RYQSLGDPAF VTAPVRGFTS KAYAAQRVKL
IDPSKATPVR DLKPGDPLKF ESPSTTHFSV ADSEGNAVST TYTLGSDFGS GVMIAGTGIL
LNNQMNNFSH EQAWQARRKG TPPPLNAMAP GKRMLSTMMP TMVFKDGKPW LIIGTPGGST
IITTMLQLVV NTVDFGLNVE EATHQPRIYQ GTTAALRVEP NFNPDTVAAL KAKGHRIDMD
ETMGSAQSIM ITDKLFLGAA DPRRPGARAV EP
//
