ID C5FID5_ARTOC Unreviewed; 572 AA.
AC C5FID5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=MCYG_01934 {ECO:0000313|EMBL:EEQ29115.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29115.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995702; EEQ29115.1; -; Genomic_DNA.
DR RefSeq; XP_002849000.1; XM_002848954.1.
DR AlphaFoldDB; C5FID5; -.
DR STRING; 554155.C5FID5; -.
DR GeneID; 9229052; -.
DR VEuPathDB; FungiDB:MCYG_01934; -.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_0_1; -.
DR OMA; ICGMGPP; -.
DR OrthoDB; 2910309at2759; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000002035; 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 PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF62; GLUTATHIONE HYDROLASE; 1.
DR Pfam; PF01019; G_glu_transpept; 2.
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:UP000002035};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368068}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..572
FT /note="Glutathione hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002951626"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 572 AA; 62338 MW; 091EF4EBEC148EF7 CRC64;
MLFPTIFSAL LQSTVLVAAS AIPPVPNAGG NGGDTTSQQT RGITIASESQ YCNDKATELF
RENPEATAAD ALINTVLCIG PGIGGGGFAL VKSGDKFEAI DFRPTAPSSA TDEYYDTHGV
HTGGASSGVP AELKGLREIY KYGKLPWKSL FQPAIKAAKG DFKANDDMIY FIQHVLDDSP
LDFTALANPH CGWLGQYPWN ETFCPHGELM RKGTPLNRAK YATTLDAIAN SGSEDIFYNG
YIADHTYNTL HVVLSILKVL EKFMGMFNPG ADKLSTHWLI EALRFGYAQR SRLGDPDPKF
DPNINIDAYQ KWLIDEKNGF PHNVKIQDKA QSNPQSYILP YPGSSQEPSS SPSDDAVKYT
GGTSHVVALD NNGLAIALTT SVGEFFGSRI MDPTTGVIFD DVMADFQRIN HTDPLEFANN
HIAKGGKRPL SGMSPTIITD KAGHVYFITG SAGGMRIPSA TLQTIVNALD RGMSVGDALS
APRLHDQLSP NITEFDLSLT SDTRMYNKHI VKDMRDRNHR FTWVEPGFSS AQAIKWVPGH
APEASGEEWQ SDSGGCVWWD GIKNCPFKRN TD
//
