ID A0A0D9Y3B5_9ORYZ Unreviewed; 658 AA.
AC A0A0D9Y3B5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G03590.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM01G03590.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM01G03590.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D9Y3B5; -.
DR STRING; 40148.A0A0D9Y3B5; -.
DR MEROPS; T03.A01; -.
DR EnsemblPlants; OGLUM01G03590.1; OGLUM01G03590.1; OGLUM01G03590.
DR Gramene; OGLUM01G03590.1; OGLUM01G03590.1; OGLUM01G03590.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_3_1; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF9; GLUTATHIONE HYDROLASE 7; 1.
DR Pfam; PF01019; G_glu_transpept; 2.
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:UP000026961};
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 28..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 658 AA; 68382 MW; A5319DCE94683BE0 CRC64;
MAARGGLENP LLGGGAVSSP DSRRRRPCTA LAIAAAALLA LAACVVLLLA SSGGWEHGDD
RSRVVSGGGG GVRLSPHEVE AGVGAVATDD GRCSEVGAAA LRAGGHAVDA AVAATLCLGV
VHPMSSGVGG GAFIVARDAA SGDAVAFDAR ETAPAAATPD MYAGNPTSKY KGALAMGIPG
ELAGLHAAWS RYGRLPWKDL FAPAIKLARD GFTVVPYLEI ALKKTERDVL ADPGLRAVLA
PEGRILAAGE VCRNPALADT LEAIASGGVE AFYGGAVGER FVADVRRAGG IATVDDLRAY
KVEVSDAMRA DAMGYTFLGM PPPSSGGVGV ALILNILGGY KSLEFLKGFL GLHRFIEAFK
HMLAIRMDLG DPDYVNVTGN VSEMLSPAFA DKLRQRIVDN TTFPPSYYFP KWSQLDDHGT
SHLCVVDGDR NAVAMTTTEN HLFGAHLLSP STGIVVNNQM DDFSVPAEGT TPPDNLPPAP
ANFIAPGKRP LSSMTPTIIL KALTNHVADD AVTLSSPSPV LTTTITVCGF VQDGQLAGVV
GGSGGPFIIA TVVQVFVNHF IVGMHPLDAV LNPRLVPNEV VYENVTVVDG EVFELSGEAR
EFLRRRGHRL TSTDSGAVCQ FIVQDLLTPV AAAGDENVFH GMLTAVSDPR KDGRPAGM
//
