ID A0A0E0DF07_9ORYZ Unreviewed; 587 AA.
AC A0A0E0DF07;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI04G13110.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI04G13110.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI04G13110.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI04G13110.1}
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|RuleBase:RU368068}.
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DR AlphaFoldDB; A0A0E0DF07; -.
DR STRING; 40149.A0A0E0DF07; -.
DR EnsemblPlants; OMERI04G13110.1; OMERI04G13110.1; OMERI04G13110.
DR Gramene; OMERI04G13110.1; OMERI04G13110.1; OMERI04G13110.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000008021; Chromosome 4.
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 NCBIfam; TIGR00066; g_glut_trans; 1.
DR PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF34; GLUTATHIONE HYDROLASE 1-RELATED; 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|RuleBase:RU368068};
KW Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368068}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..587
FT /note="Glutathione hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002357185"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 587 AA; 62333 MW; A61531A2AB8E35B1 CRC64;
MNARRLHKWA ATARLVLLLF LLAAGAAAAA AATAGRREVV TSPHGAVAAD DGRCSRIGRD
ALRDGGNAVD AAVAASLCLG VVSPASSGVG GGAFMLVRLA DGTALAYDSR ETAPLAASQV
SARLLPITRD MYGGNATLKA RGALSIAVPG EIAGLYEAWK RHGKLPWKRL VMPAAKLARA
FRVSPYLRKQ MEATRDGILQ NKGISGVYTS NGDILNVGDV CRNTRLARTL VAVAEKGPDV
FYNGAVGDQL VKDIQEVGGI ITMEDLKKYQ VKIRRPLSEN VLGLTVLSMP PPSAGGAGLM
LVLNILTQYG LPAGFSGSLG IHRLIESLKH YFAIRMNLGD PEFVNVNEVV SDMMSPKFAA
DLKKTIYDNM TFDPKHYGGR WNILQDHGTS HLSIVDSERN AVSMTTTVNA YFGSLILSPS
TGILLNNEMD DFSMPANTSA NSPPPAPANF VRPLKRPLSS MTPTIILKDG NLKAAVGASG
GSMIPAGTME VLLNHFVKNM DPLSSVMAPR VYHQLIPNVV QYENWTTVTG DHFELDAATR
ADLQKKGHVL APLAGGTISQ LVVDDVERHG GLTAVSDPRK GGIPAGY
//
