ID A0A257B979_9BACT Unreviewed; 569 AA.
AC A0A257B979;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glutathione hydrolase proenzyme {ECO:0000256|RuleBase:RU368036};
DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368036};
DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368036};
DE Contains:
DE RecName: Full=Glutathione hydrolase large chain {ECO:0000256|RuleBase:RU368036};
DE Contains:
DE RecName: Full=Glutathione hydrolase small chain {ECO:0000256|RuleBase:RU368036};
GN Name=ggt {ECO:0000313|EMBL:OYT73424.1};
GN ORFNames=CFK52_01810 {ECO:0000313|EMBL:OYT73424.1};
OS Chloracidobacterium sp. CP2_5A.
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=2012633 {ECO:0000313|EMBL:OYT73424.1, ECO:0000313|Proteomes:UP000216393};
RN [1] {ECO:0000313|EMBL:OYT73424.1, ECO:0000313|Proteomes:UP000216393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP2_5A {ECO:0000313|EMBL:OYT73424.1};
RA Ward L.M., Mcglynn S.E., Fischer W.;
RT "Draft genome of Chloracdibacterium sp. CP2_5A, a phototrophic
RT Acidobacteria from a Japanese hot spring.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001049,
CC ECO:0000256|RuleBase:RU368036};
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|ARBA:ARBA00000250,
CC ECO:0000256|RuleBase:RU368036};
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|ARBA:ARBA00001089,
CC ECO:0000256|RuleBase:RU368036};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- SUBUNIT: This enzyme consists of two polypeptide chains, which are
CC synthesized in precursor form from a single polypeptide.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000256|RuleBase:RU368036}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYT73424.1}.
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DR EMBL; NKPT01000003; OYT73424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257B979; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000216393; 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:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
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; PTHR43881; GAMMA-GLUTAMYLTRANSPEPTIDASE (AFU_ORTHOLOGUE AFUA_4G13580); 1.
DR PANTHER; PTHR43881:SF1; GAMMA-GLUTAMYLTRANSPEPTIDASE (AFU_ORTHOLOGUE AFUA_4G13580); 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU368036};
KW Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036};
KW Hydrolase {ECO:0000256|RuleBase:RU368036};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU368036, ECO:0000313|EMBL:OYT73424.1};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..569
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013101380"
FT REGION 488..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 569 AA; 61532 MW; 0E463354292CE007 CRC64;
MRRIWAWALG FLALAGAGAA RTAAPDRITG RPFATRSEVI ARHGLACTSQ PLATQVAVDI
LKRGGTAVDA AIAANAVLGL VEPTGCGVGG DLFALVWDPK TRRLHGLNAS GRSPKRLTLD
EFRRRGLKRI PSFGPLPVTA PGCVDGWFAL HARFGALPMK ELLAPAIAYA REGFPVSELI
AYYWERNAAA LAQFPNVREV YAPGGRTPRK GELFRNPQLA TTLEKIAAGG RDAFYKGEIA
GVIADFIARQ GGFLDREDLA AHASEWVEPI STNYRGYDVW ELPPNGQGLA ALQMLNILEG
YDLAKFGFGS REHLHYFVEA KKLAYEDRAK YYADPAFASV PVAGLLSKAY AAERRKLIHP
QRAGTRREAG DPALQTGDTI YLTTADRNGM MVSLIQSNYR GMGSGMVPDG LGFMLHDRGE
MFALEEGHAN VYAPGKRPFH TIIPAFVTKD GQPFLSFGVM GGGFQPLGHV QILINIIDFG
MNVQEAGDAP RIDHQGSSEP TGERATGGGT VTLETGFSYE IIRELIRAGH RVGFAVGDYG
GYQAIRWDAE QGVYYGASES RKDGQAAGY
//
