ID B8MW63_ASPFN Unreviewed; 584 AA.
AC B8MW63;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
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};
GN ORFNames=AFLA_074100 {ECO:0000313|EMBL:EED56716.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED56716.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED56716.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- FUNCTION: Gamma-glutamyltransferase. {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: Mycotoxin biosynthesis. {ECO:0000256|RuleBase:RU368068}.
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DR EMBL; EQ963472; EED56716.1; -; Genomic_DNA.
DR RefSeq; XP_002372328.1; XM_002372287.1.
DR AlphaFoldDB; B8MW63; -.
DR STRING; 332952.B8MW63; -.
DR MEROPS; T03.011; -.
DR EnsemblFungi; EED56716; EED56716; AFLA_074100.
DR VEuPathDB; FungiDB:AFLA_002956; -.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_0_1; -.
DR OMA; KATKNMF; -.
DR Proteomes; UP000001875; 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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368068}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..584
FT /note="Glutathione hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002875558"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 584 AA; 62966 MW; 4E1A4C3A16073F35 CRC64;
MYRFLRNTLS LSFILVLALI HLPDVLSSPL EPSAHYDSRS ANTVEHFEEG KLGAVASESA
ICSRHGTEML KIGGNAADAV IATIFCVGVV GMYHSGIAGG GFMLVRAPNG SYEFIDFRET
APAAAFEEMF KNNTDASTSG GLASGVPGEV RGLEYLHKKY GSLPWSTVMQ PAIQTARQGF
PVGRDLVRYM NSAVGDGEDF LSKDPTWAID FAPNGTRLGL GDTITRKRYA DTLETIANNG
PDAFYTGPIA ETMIQALQAA NGTMTLEDLR NYTIAIRDTS QIDYRGYRVI GTSAPSSGTV
ALNILKVLDT YDSFMVPDNV NLSTHRLDEA IRFGYGLRTE LGDPYFLEGL DEYQKDMLEQ
STIDEIRGKI SDLHTQNVSA YDPKGLESLD TPGTSHIAAV DHTGLTISTI TTINLLFGSK
VMVPETGIIM NNEMDDFSTP GSSNAFGYVP SEANFIRPGK RPLSSITPTI VTHQNGSVFF
VAGSAGGSRI ITATVQNIIH AVDEGLSAAE ALARPRLHDQ LIPNQVRFEY AYNNETVAFM
KSLGHNVTWV APGDSTAQAI RVLPNGTFDA AGEPRQLDSG GFAV
//
