ID W6MEK2_9GAMM Unreviewed; 599 AA.
AC W6MEK2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-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 Name=ggt {ECO:0000313|EMBL:CDI04758.1};
GN ORFNames=BN873_p60018 {ECO:0000313|EMBL:CDI04758.1};
OS Candidatus Competibacter denitrificans Run_A_D11.
OG Plasmid pCD {ECO:0000313|EMBL:CDI04758.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Competibacter.
OX NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI04758.1, ECO:0000313|Proteomes:UP000035760};
RN [1] {ECO:0000313|EMBL:CDI04758.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI04758.1,
RC ECO:0000313|Proteomes:UP000035760};
RC PLASMID=pCD {ECO:0000313|EMBL:CDI04758.1};
RA McIlroy S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI04758.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI04758.1,
RC ECO:0000313|Proteomes:UP000035760};
RC PLASMID=pCD {ECO:0000313|EMBL:CDI04758.1};
RA McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT functional metabolic diversity.";
RL Submitted (FEB-2014) 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:CDI04758.1}.
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DR EMBL; CBTJ020000118; CDI04758.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MEK2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000035760; 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.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 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 Plasmid {ECO:0000313|EMBL:CDI04758.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 411
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 599 AA; 63734 MW; 32F67AC77F1FDCB3 CRC64;
MRSRRDRSPV FLPPEISMPR WPSSVRPPAR LLGGVAALLL SLGAVAGGTE PALFDTRDRI
HPVHARHGLV VAQEALASQV GLAVLRGGGH AADAAVAVGF ALAVTLPQAG NLGGGGFLLV
YDDGKKQTEA IDFRETAPAA VGRDFYLNER GEVDEARIRH SHQAAGVPGT VAGLALAHAR
HGRLPWRSLL EPAIRLAEQG FPVGPELARS LREARERMAP WPASAKAFFK PDGSAYSPGE
TLLQPDLAAS LKLIAEEGSR AFYEGEIARK LVADMQEHRG AIIADDLRGY RAVIRAPVRG
TYRGYEIASM PPPSSGGVHL VQILNVLETW SLGDLGHNGA ATIHRLAEAT KLAYADRSEY
LGDPDFAKVP VAGLTSKAYA RELAARIDPN RAKPAAQIKP GQPHRFESEQ TTHYSVVDRD
GNAVAVTYTL NFPYGSGIVA AGTGILLNNE MDDFAAKPGV PNAYGLIGGD ANAVGPGKRP
LSSMAPTLVF KDGRLVLVAG SPGGSRIITA VLQVLSNVID HRLNLAEATV APRVHHQWSP
DELRVEEGLS PDTVRLLESL GHKVVIREAM GDTQSILRAP EGWYGFSDTR QPGGLAAGY
//
