ID A0A1X3DEP0_9NEIS Unreviewed; 575 AA.
AC A0A1X3DEP0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=BWD09_03215 {ECO:0000313|EMBL:OSI18245.1};
OS Neisseria dentiae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=194197 {ECO:0000313|EMBL:OSI18245.1, ECO:0000313|Proteomes:UP000193118};
RN [1] {ECO:0000313|Proteomes:UP000193118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19151 {ECO:0000313|Proteomes:UP000193118};
RA Wolfgang W.J., Cole J., Wroblewski D., Mcginnis J., Musser K.A.;
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|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:OSI18245.1}.
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DR EMBL; MTBO01000004; OSI18245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3DEP0; -.
DR STRING; 194197.BWD09_03215; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000193118; 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:UP000193118};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 395
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 575 AA; 61098 MW; 04E15DEFF8DE999B CRC64;
MLGLLAAFSL TAHAYQPAPA AENHAPEQGT GKTAQQLVEA KEFMAASTNP LATEAGYEVL
KRGGSAIDAM IAMQTTLSLT EPQSSGLGGG AFLVYWDNQA KKLTTFDARE TAPQAATPQL
FLDENGKPLE FMQAVVGGRS VGVPGVPKLL EDVHKRYGKL PWKTLFAKPV ALAERGFAVS
PRMAKSIEQN RQYLQRYPET AAYFLPGGKP PAAGDVLKNP KFAASVKLLA AKGSAPFYRG
KPAENIIKAV NGAKDNPGKI TAADLRNYRI IEREPVCAPY REFEICGMDA PSSGGIALAQ
IFGVMRHFDM KAMGAGNIQS WRVLGDASRL AFADRDYYVA DPAFADVPVR AMLHPEYLKL
RAGLIANSYG ALPQVSPGGF ARTQGKGQGM ELPSTSHIAV VDKSGNVVSM TTSIENAFGS
TLMANGYLLN NELTDFAFNP VDAEGKTVAN SVAGGKRPRS SMAPTIVMKN GEPYMAVGSP
GGSRIIGYVA KTLTAHIDWG MDIQAAIDLP NMLNRGSAYE LEENSAAAAK APDLEKLGYK
VQVRDLNSGV QGIVIGKTGL QGGADPRREG QVMGD
//
