ID A0A1G4K724_9SACH Unreviewed; 612 AA.
AC A0A1G4K724;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glutathione hydrolase {ECO:0000256|RuleBase:RU368068};
DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368068};
DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368068};
DE AltName: Full=Gamma-glutamyltransferase {ECO:0000256|RuleBase:RU368068};
DE AltName: Full=Gamma-glutamyltranspeptidase {ECO:0000256|RuleBase:RU368068};
GN ORFNames=LANO_0F03136G {ECO:0000313|EMBL:SCU99675.1};
OS Lachancea nothofagi CBS 11611.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU99675.1};
RN [1] {ECO:0000313|EMBL:SCU99675.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11611 {ECO:0000313|EMBL:SCU99675.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC glutathione conjugates. {ECO:0000256|RuleBase:RU368068}.
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|RuleBase:RU368068};
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|RuleBase:RU368068};
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|RuleBase:RU368068};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000256|ARBA:ARBA00005115, ECO:0000256|RuleBase:RU368068}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT598452; SCU99675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4K724; -.
DR OrthoDB; 2910309at2759; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000189911; Chromosome f.
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: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; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF9; GLUTATHIONE HYDROLASE 7; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU368068}; Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368068}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..612
FT /note="Glutathione hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009236397"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 612 AA; 67677 MW; E153283FF4FAD353 CRC64;
MVALRNLLVV FPLVSMTSCM QHYFVQSSDH NIDIKPLPRQ PTLNPNSSQV LRTGRSGAIS
SDSEFCSSIA VEKVLKKFEN ANAADAAVTV ALCLGMKNFF SSGIGGGGYA VFVGGNKQEK
RLDPLFLDFR EQAPELAHKD MFAQTPNASQ VGGLAVGIPG ELKGLYELYS QRGSGHVQWH
ELLEPIIHLG TKGWPVDEIT ALVLKMYEPY FVEHRHDWKF VLNSAGNETL KIGDNLKRTA
LAQTLREIAQ NGTAAPFYDP NHRIGKALVN KVQKSGGILT DHDLEAYYVN ISQPLSTKIR
AGWANVPNND LEVFTSSGSS SGAALVSALK ILDHFPSLSG GDYIPEQTYV LIECMKYMSS
ARSRLGDYSQ QDKLPDRVEE VLNSDWIESA VKTIKENMDS LQTLSNWTDY HPMYEMTDPH
GTTHFSVVDK FNNAVSLTST VNLLFGSLVH DTETGILLNN QMDDFSQPHR SNAFGLAPSK
YNFAEPGKRP LSSSSPVIVL NELDQPDLVI GASGGSRITP SIFQVMTRLY WYNMPLLEAI
AYPRVHHQLL PDQLEIESFG MLGKSTIDSL RLMGHDLVEQ APKSVVNGIK QSVGEWHAVS
DFWRKRGISI AY
//
