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Database: UniProt
Entry: A0A2K2ADH0_POPTR
LinkDB: A0A2K2ADH0_POPTR
Original site: A0A2K2ADH0_POPTR 
ID   A0A2K2ADH0_POPTR        Unreviewed;       583 AA.
AC   A0A2K2ADH0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=POPTR_005G082800 {ECO:0000313|EMBL:PNT35576.1};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:PNT35576.1, ECO:0000313|Proteomes:UP000006729};
RN   [1] {ECO:0000313|EMBL:PNT35576.1, ECO:0000313|Proteomes:UP000006729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729};
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA   Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA   Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA   Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA   Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA   Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA   Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA   Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA   Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA   Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA   Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA   Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA   Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA   Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA   Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA   Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA   Rokhsar D.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
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   EMBL; CM009294; PNT35576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K2ADH0; -.
DR   EnsemblPlants; Potri.005G082800.2.v4.1; Potri.005G082800.2.v4.1; Potri.005G082800.v4.1.
DR   Gramene; Potri.005G082800.2.v4.1; Potri.005G082800.2.v4.1; Potri.005G082800.v4.1.
DR   OMA; KATKNMF; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000006729; Chromosome 5.
DR   ExpressionAtlas; A0A2K2ADH0; baseline and differential.
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:UP000006729};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU368068}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..583
FT                   /note="Glutathione hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014451686"
FT   ACT_SITE        379
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ   SEQUENCE   583 AA;  63269 MW;  945288B984C10756 CRC64;
     MSSLPSLWAI LLFFLFLLCP ATSSLHGRQS GSTKFRHQEV VARHGAVATD DGRCSRIGID
     VLREGGHAVD AAVAASLCLG VVSPASSGIG GGAFMLIRLA SGEVHAYDMR ETAPMQASEN
     MYDGNDTLKA RGALSIAVPG ELAGLYKAWK QHGRLPWERL VRPAEKLARR GFKISRYLRM
     QMEKTQSGIL ADEGLRNVFT SNGDLLQQGD ICYNKKLADT LRKISKGVEA FYNGPIGFNL
     VRDIQKLGGI LTIEDLQRYK VRVREPIITN ILGYKIIGMP PPSSGGASMM LILNILAQYG
     VPEGISGPLG FHRLVESLKH AFAVRMKLGD PDFADVAQVV SDMISPKFAE ELKKTIYDNM
     TFDPGHYGGR WNQINDHGTS HISIVDSERN AVSMTNTVNS YFGTQILSPS TGIVLNNEMD
     DFSMPGNNTG HVPPPAPLNL IRPGKRPLSS MTPTIVLKDE QLKGVVGASG GSMIIAGTTE
     VLLNHFAKGM DPLSSVLAPR VYHQLTPNVV QYENWTTVYG DHFELSADVR AFLQKRGHVL
     KGIAGGTICQ FIVQDLETTE GNKLMGKLVA VSDPRKGGLP AGY
//
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