ID A0A0E0PA17_ORYRU Unreviewed; 573 AA.
AC A0A0E0PA17;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI04G16120.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI04G16120.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; A0A0E0PA17; -.
DR STRING; 4529.A0A0E0PA17; -.
DR EnsemblPlants; ORUFI04G16120.1; ORUFI04G16120.1; ORUFI04G16120.
DR Gramene; ORUFI04G16120.1; ORUFI04G16120.1; ORUFI04G16120.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_3_1; -.
DR OMA; KATKNMF; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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:UP000008022};
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..573
FT /note="Glutathione hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002370064"
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 573 AA; 61061 MW; 6D1FF482EC15A605 CRC64;
MNARRLHKWA ATARLVLLLL AAAAAAAAAA GRREVVTSPH GAVAADDGRC SRIGRDALRD
GGNAVDAAVA ASLCLGVVSP ASSGVGGGAF MLVRLADGTA LAYDSRETAP LAASQDMYGG
NETLKARGAL SIAVPGEIAG LYEAWKRHGK LPWKRLVMPA AKLARAFRVS PYLRKQMEAT
RDGILQNKGI SGVYTSNGDI LNVGDVCRNI RLARTLVAVA EKGPDVFYKG AVGDQLVKDI
QEVGGIITME DLKKYQVKIR RPLLENVLGL TVLSMPPPSA GGAGLMLVLN ILTQYGLPAG
FSGSLGIHRL IESLKHYFAI RMNLGDPEFV NVNEVVSDMM SPKFAADLKK TIYDNTTFDP
KHYGGRWNIL QDHGTSHLSI VDSERNAVSM TTTVNAYFGS LILSPSTGIL LNNEMDDFSM
PANTSANSPP PAPANFVRPL KRPLSSMTPT IILKDGNLKA AVGASGGSMI PAGTMEVLLN
HFVKNMDPLS SVMAPRVYHQ LIPNVVQYEN WTTVTGDHFE LDAATRADLR RKGHVLEPLA
GGTISQLVVD DVERYGGLTA VSDPRKGGFP AGY
//
