GenomeNet

Database: UniProt
Entry: A0A093YRV0_9PEZI
LinkDB: A0A093YRV0_9PEZI
Original site: A0A093YRV0_9PEZI 
ID   A0A093YRV0_9PEZI        Unreviewed;       577 AA.
AC   A0A093YRV0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=V492_07025 {ECO:0000313|EMBL:KFY07559.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY07559.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY07559.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY07559.1,
RC   ECO:0000313|Proteomes:UP000029299};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY07559.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPJU01002524; KFY07559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093YRV0; -.
DR   STRING; 1420902.A0A093YRV0; -.
DR   HOGENOM; CLU_014813_4_0_1; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000029299; Unassembled WGS sequence.
DR   GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
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:SF62; GLUTATHIONE HYDROLASE; 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:UP000029299};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU368068}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..577
FT                   /note="Glutathione hydrolase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001889653"
FT   ACT_SITE        387
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ   SEQUENCE   577 AA;  62328 MW;  48E34E2EF5274DC2 CRC64;
     MHGFLGQANP GRSSNTRWRF ALLSLLALLP PPSVEASIVL SRDGTRGAVA SESSICSNIG
     IDLIRRGGNA ADAAVGTTLC VGVIGMYHSG IGGGGFMLVR SETGEYEDVD FRETAPSAAY
     EDMYANFTIG SIVGGDASGV PGELRGFEYL HKKYGKLPWA MVVMPAAKVA ERGFTVTEDL
     YGFMIGREKL GQYFLTEDPS WAMDFAPKGR LLQPGELMTR KRLGKTLRTI AKQGASAFYE
     GPIADATIRA LQLANGSMTL DDMSKYEIIT RKPVSIDYRG YKIFSTGAPS SGAVALNTFK
     IIEGYNMSDP DNLNLNTHRL DEAIKFSYGN RNELGDPDFV EGIADFQSQM LDTANASATR
     NKISDDHTLD PTAYNPKRLS HPDSHGTSHV VTSDASGLSI TLTTTVNLSF GSRLCVPETG
     IIMNNEMNDF SIPGVSNEFG FVPSPNNYIR PGKRPLSSIT PVIVEQADGS LYVVTGAAGG
     SRIITATIQA LWHVLDHGMT MPEALAQPRL DDQLLPAQVR FELGYDNATT AYMRAKGHNV
     TWTSELLSKT QGIRRLENGT FEAAAEPRQK NSGGYAV
//
DBGET integrated database retrieval system