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Database: UniProt
Entry: A0A0P0CGM7_9BACT
LinkDB: A0A0P0CGM7_9BACT
Original site: A0A0P0CGM7_9BACT 
ID   A0A0P0CGM7_9BACT        Unreviewed;       548 AA.
AC   A0A0P0CGM7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=DC20_00655 {ECO:0000313|EMBL:ALJ01090.1};
OS   Rufibacter tibetensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ01090.1, ECO:0000313|Proteomes:UP000061382};
RN   [1] {ECO:0000313|EMBL:ALJ01090.1, ECO:0000313|Proteomes:UP000061382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1351 {ECO:0000313|EMBL:ALJ01090.1,
RC   ECO:0000313|Proteomes:UP000061382};
RA   Dai J.;
RT   "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT   radiation-resistant bacterium from tibet plateau.";
RL   Submitted (AUG-2015) 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|ARBA:ARBA00009381, ECO:0000256|RuleBase:RU368036}.
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DR   EMBL; CP012643; ALJ01090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0CGM7; -.
DR   STRING; 512763.DC20_00655; -.
DR   KEGG; rti:DC20_00655; -.
DR   PATRIC; fig|512763.3.peg.143; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000061382; Chromosome.
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; PTHR43199; GLUTATHIONE HYDROLASE; 1.
DR   PANTHER; PTHR43199:SF1; GLUTATHIONE HYDROLASE PROENZYME; 1.
DR   Pfam; PF01019; G_glu_transpept; 1.
DR   PRINTS; PR01210; GGTRANSPTASE.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU368036};
KW   Glutathione biosynthesis {ECO:0000256|RuleBase:RU368036};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061382};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW   Zymogen {ECO:0000256|RuleBase:RU368036}.
FT   ACT_SITE        358
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ   SEQUENCE   548 AA;  58941 MW;  57DA1CBB52F22509 CRC64;
     MGCTNRNLHK TGLVADKAMV VTAHPLASAV GAQILKRGGN AVDAAVAVQF ALAVVYPDAG
     NIGGGGFLVL RQKDGSINAL DYREKAPAKA HRDMYLNGQG EVIENLSYKG HLAAGVPGTV
     DGMVQAHEKY GSLPWTDLVQ PAVLLAAKGF PLTQKEAKKL NEQRKDFLQF NTQRPEFILK
     NRWREGDTLR LLDLAHTLER IRDKGRAGFY EGPTAALITA EMERGKGIIS KTDLANYRSV
     WRTPIAGQVG VYRVISMPPP SSGGIALIQL LTIAQDYPLK DWGWNTVATS HLMVEAERRI
     YADRARHFGD ADFYEVPVKG LLNPAYIKSR MKGYTPKKAT PSEEVSAGVP PLPEGPNTTH
     YSIVDAQGNA VSVTTTLNSS FGNKVFVAGA GFLLNNEMDD FSIKPGFPNS YGLIGEEANA
     IAPGKRMLSS MTPTILEKDG KLFMVIGAMG GSTIITTVYQ IIQNVTVHGH TMQGAVNAGR
     FHHQWKPNWI LTEWGALGPL TGAGLWIKGH KIAPKYGGIG RAAGILVLPN GKLEGGADPR
     GDDAAAGF
//
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