ID A0A251NGY2_PRUPE Unreviewed; 623 AA.
AC A0A251NGY2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PRUPE_7G216500 {ECO:0000313|EMBL:ONH97889.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH97889.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONH97889.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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}.
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DR EMBL; CM007657; ONH97889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251NGY2; -.
DR STRING; 3760.A0A251NGY2; -.
DR EnsemblPlants; ONH97889; ONH97889; PRUPE_7G216500.
DR Gramene; ONH97889; ONH97889; PRUPE_7G216500.
DR eggNOG; KOG2410; Eukaryota.
DR OrthoDB; 2910309at2759; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000006882; Chromosome g7.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU368068}; Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368068};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 592..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 623 AA; 66888 MW; 51875B3B4DDB1DF7 CRC64;
MAQQSLAAPL LDSHGSTTSR AFWLLLAFVA IIFVGFIFGG HTNGRVLIRG ANNYNEGNFK
INDSDIVESE KGVVAADDAR CSEVGASILR QGGHAVDAAV GTALCLGVVN SMASGIGGGG
FMLVRSSATS QTQAFDLRET APIAASQNMY ETNPKAKLLG ALSMGVPGEI AGLHEAWLQH
GRMAWKTLFQ PAIKLAKDGY VIAPYLGGYI SRFGDKILSD PGLRQVFAPN GKLLQTGDTC
YNVELGHSLE AVAELGPQTF YNGSVGEKLV KDVREAGGIL TMEDLRNYKV SVVEPVAANV
MGYNVFGMPP PSSGTLGLSL VLNIFDSYGT SDAAKGDLGL HRLIEALKHM FAVRMNLGDP
AFVDTSKYAS DMLSSSFAKK IQQKIFDNTT FPPEYYLQRW SQLRDHGTSH FCIVDADRNA
VSMTSTVNYP FGGGVLSPST GILLNNEMDD FSTPTEISPD RLPPAPANFI EPNKRPLSSM
TPLIIMKDNE LAGVIGGSGG MNIIPAVTQV FLNYFVLGME PLAAVQSPRI YHKLIPNVVS
YENLTLIDGD HIELSDEKKL FLQERGHQLE AKAGGAITQL VVQTLRKPVN MGRKSGQNSN
EQTFHGTLTA VSDPRKDGKP AAV
//
