GGT1_ARTBC
ID GGT1_ARTBC Reviewed; 584 AA.
AC D4B387;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Glutathione hydrolase proenzyme {ECO:0000250|UniProtKB:P19440};
DE EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltransferase ARB_02921 {ECO:0000305};
DE EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltranspeptidase {ECO:0000250|UniProtKB:P19440};
DE Short=Gamma-GT {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Leukotriene-C4 hydrolase {ECO:0000250|UniProtKB:P19440};
DE EC=3.4.19.14 {ECO:0000250|UniProtKB:P19440};
DE Contains:
DE RecName: Full=Glutathione hydrolase heavy chain {ECO:0000250|UniProtKB:P19440};
DE Contains:
DE RecName: Full=Glutathione hydrolase light chain {ECO:0000250|UniProtKB:P19440};
DE Flags: Precursor;
GN ORFNames=ARB_02921;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione
CC (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl
CC compounds. The metabolism of glutathione releases free glutamate and
CC the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and
CC glycine by dipeptidases. In the presence of high concentrations of
CC dipeptides and some amino acids, can also catalyze a transpeptidation
CC reaction, transferring the gamma-glutamyl moiety to an acceptor amino
CC acid to form a new gamma-glutamyl compound. Initiates extracellular
CC glutathione (GSH) breakdown, provides cells with a local cysteine
CC supply and contributes to maintain intracellular GSH level. It is part
CC of the cell antioxidant defense mechanism.
CC {ECO:0000250|UniProtKB:P19440}.
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:0000250|UniProtKB:P19440};
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:0000250|UniProtKB:P19440};
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:0000250|UniProtKB:P19440};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4;
CC Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC site is located in the light chain. {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit and the
CC autocatalytic cleavage is essential to the functional activation of the
CC enzyme. {ECO:0000250|UniProtKB:P19440}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; ABSU01000032; EFE30242.1; -; Genomic_DNA.
DR RefSeq; XP_003010882.1; XM_003010836.1.
DR AlphaFoldDB; D4B387; -.
DR SMR; D4B387; -.
DR STRING; 663331.D4B387; -.
DR MEROPS; T03.011; -.
DR EnsemblFungi; EFE30242; EFE30242; ARB_02921.
DR GeneID; 9524997; -.
DR KEGG; abe:ARB_02921; -.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_4_0_1; -.
DR OMA; KATKNMF; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glutathione biosynthesis; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..394
FT /note="Glutathione hydrolase heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT /id="PRO_5003053881"
FT CHAIN 395..584
FT /note="Glutathione hydrolase light chain"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT /id="PRO_0000435284"
FT ACT_SITE 395
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 120
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 413
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 434
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 465..466
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 584 AA; 63768 MW; F0B5A620D10EC21F CRC64;
MAPAAMNLLC TVLYLLSSFA QVSDAAPWLF SRSIPASYHD GRLGAVASEN SMCSEYGADM
LKIGGNAADA VCIYRLSLFF AFLPYPALQE DRAMYHSGIG GGGFMLIRAP NGTYEFIDFR
ETAPAAAFQD MFKNNTSGST SGGLASGVPG EVRGLEYLHK NYGKLPWKTV MEPAIRTARD
GFRVTEDLSR IMLHSTKNGN FLAENAAWAL DFAPQGTLLK VGDIITRRRY GDTLDKIAKY
GADAFYTGPM AQAMVNALRA ANGTMTLEDL KNYTVVSRPT AQIEYRGMTV TSTTAPSSGV
VLLSILKLLN GYKNFFRMDP GPLSTHRMDE AIRFGYGQRT ELGDPLFFSN LTDYQKKMIS
DEAANKNRMN ISDEYTQDIA VYDPKGLESL NTPGTSHIST ADRSGMAVSL TTTINLYFGS
RVIVPETGII MNNEMDDFSV PGRSNSFGYK PSPSNFIRPG KRPLSSICPT IITRPDGSLY
FVSGAAGGSQ IITGTLQSVI NVMDRKMNVR QALKAPRLHD QLVPNVALME DEFDKKTVDF
MISRKHNVTR EKSGSTVESI MRLKNGVFEA SGEPRLANSG GVVV
