ID   GGT_SYNY3               Reviewed;         518 AA.
AC   P74181;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Glutathione hydrolase proenzyme;
DE            EC=3.4.19.13;
DE   AltName: Full=Gamma-glutamyltranspeptidase proenzyme;
DE            EC=2.3.2.2;
DE   Contains:
DE     RecName: Full=Glutathione hydrolase large chain;
DE   Contains:
DE     RecName: Full=Glutathione hydrolase small chain;
DE   Flags: Precursor;
GN   Name=ggt; OrderedLocusNames=slr1269;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- 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   -!- 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   -!- 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   -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA18270.1; -; Genomic_DNA.
DR   PIR; S75811; S75811.
DR   AlphaFoldDB; P74181; -.
DR   SMR; P74181; -.
DR   STRING; 1148.1653356; -.
DR   MEROPS; T03.013; -.
DR   PaxDb; P74181; -.
DR   EnsemblBacteria; BAA18270; BAA18270; BAA18270.
DR   KEGG; syn:slr1269; -.
DR   eggNOG; COG0405; Bacteria.
DR   InParanoid; P74181; -.
DR   OMA; VCGMGPP; -.
DR   PhylomeDB; P74181; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000001425; Chromosome.
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.
PE   3: Inferred from homology;
KW   Acyltransferase; Glutathione biosynthesis; Hydrolase; Protease;
KW   Reference proteome; Signal; Transferase; Zymogen.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..336
FT                   /note="Glutathione hydrolase large chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011056"
FT   CHAIN           337..518
FT                   /note="Glutathione hydrolase small chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011057"
FT   ACT_SITE        337
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   518 AA;  55988 MW;  4FDA234F16C66540 CRC64;
     MAGKTTGVVA AGHAQTAEAG KCMLEEGGNA FDAAIASVLA ACVVESSLTS LGGGGFLLAQ
     TAAKKSYLFD FFCQTPQVNP GEKAVDFYPV ALNFGGAWQT FHIGKGAIAV PGMVAGLFAA
     HRKLGQLPFK VLIEPAVAYA RQGFTLNRFN DFTNGLLEPI LTQQEEGRKF YAPQGKILRQ
     GEKAYLPQFA DVLEQLARHG PDWFYRGELT EWVLESLGEA SALTAKDWAD YQVEIRLPLR
     AQYRQRQLLT NPPPSAGGIL IAFALQLLEK YDLSQYPLGS AAQIQLFSQV MALSNQARRQ
     YLDGNLHCGD IEAKFLGGDR LASELGQSKF INKLGSTTHI SVLDGEGNAA SLTSSNGEGS
     GHFIPGTGIM LNNMLGEEDL NPQGFYQWPP GQRLSSMMAP TILLDQEQPR LVLGSGGSNR
     IRSAILQVVC HHLDYQLPLA EAVGRERIHW EAHKLDLEPT SVADILAQLR FDDGTQGTLW
     TEQNMFFGGV HGVATTTAGT MEGVGDPRRS GAVAYSLE