GGT_PSEUA
ID GGT_PSEUA Reviewed; 575 AA.
AC P36267;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Glutathione hydrolase proenzyme;
DE EC=3.4.19.13 {ECO:0000269|PubMed:7765305};
DE AltName: Full=Gamma-glutamyltranspeptidase proenzyme;
DE EC=2.3.2.2 {ECO:0000269|PubMed:7765305};
DE Contains:
DE RecName: Full=Glutathione hydrolase large chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase small chain;
DE Flags: Precursor;
GN Name=ggt;
OS Pseudomonas sp. (strain A14).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=69010;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RC STRAIN=A14;
RX PubMed=7765305; DOI=10.1021/bp00021a012;
RA Ishiye M., Yamashita M., Niwa M.;
RT "Molecular cloning of the gamma-glutamyltranspeptidase gene from a
RT Pseudomonas strain.";
RL Biotechnol. Prog. 9:323-331(1993).
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; Evidence={ECO:0000269|PubMed:7765305};
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:0000269|PubMed:7765305};
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:0000269|PubMed:7765305};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized in precursor form from a single polypeptide.
CC {ECO:0000269|PubMed:7765305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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DR EMBL; S63255; AAC60442.1; -; Genomic_DNA.
DR AlphaFoldDB; P36267; -.
DR SMR; P36267; -.
DR MEROPS; T03.001; -.
DR UniPathway; UPA00204; -.
DR GO; GO:0042597; C:periplasmic space; 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 SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Glutathione biosynthesis;
KW Hydrolase; Periplasm; Protease; Signal; Transferase; Zymogen.
FT SIGNAL 1..24
FT CHAIN 25..375
FT /note="Glutathione hydrolase large chain"
FT /id="PRO_0000011054"
FT CHAIN 376..575
FT /note="Glutathione hydrolase small chain"
FT /id="PRO_0000011055"
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 447..448
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 468..469
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 61301 MW; CF2EB69F02CD0201 CRC64;
MKNQTFSKAL LATALSCALF NVHAASQAPV GAENGMVVTA QHIASKVGVE VLKSGGNAID
AAVAVGYALA VVYPAAGNIG GGGFMTIQLA DGRKTFLDFR EKAPLAATAN MYLDKDGNVI
KGASTTGYLA VGVPGTVSGM EYAREKYGTK TRQQLISPAI TLADKGFVLE QGDVDMLWTS
TKDFEKDRAN SGAIFMNKGQ PFQPGERLVQ KDLARTLRLI SAKGTDGFYK GEVADKLVAS
MKAGGGIITQ ADLDQYKTRE LAPVECDYRG YHVVSAPPPS SGGVVICEIM NILEGYPMKE
LGYHSAQGVH YTIEAMRHAY VDRNSYLGDP DFVKNPLAHL LDKDYAAKIR AAINPQKAGI
SQEIKPGVPP HEGSNTTHYS IVDKDGNAVS VTYTLNDWFG AKVMANGTGV LLNDEMDDFT
SKVGVPNMYG LIQGEANAIG PGRRPLSSMS PTIVTKDGKT VMVVGTPGGS RIITATLLTM
LNMIDYGMNL QEAVDAPRFH QQWMPESTNI EAFALSPDTQ KILESWGQKF AGPQPANHIA
AILVGAPSLG GKPIGKNRFY GANDPRRNTG LALGY
