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Database: UniProt
Entry: A0A1H6G9J8_9SPHN
LinkDB: A0A1H6G9J8_9SPHN
Original site: A0A1H6G9J8_9SPHN 
ID   A0A1H6G9J8_9SPHN        Unreviewed;       563 AA.
AC   A0A1H6G9J8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05428974_3634 {ECO:0000313|EMBL:SEH19757.1};
OS   Sphingopyxis sp. YR583.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1881047 {ECO:0000313|EMBL:SEH19757.1, ECO:0000313|Proteomes:UP000198829};
RN   [1] {ECO:0000313|EMBL:SEH19757.1, ECO:0000313|Proteomes:UP000198829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR583 {ECO:0000313|EMBL:SEH19757.1,
RC   ECO:0000313|Proteomes:UP000198829};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNWK01000004; SEH19757.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6G9J8; -.
DR   STRING; 1881047.SAMN05428974_3634; -.
DR   OrthoDB; 9781342at2; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000198829; 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; 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.
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   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW   Zymogen {ECO:0000256|RuleBase:RU368036}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..563
FT                   /note="Glutathione hydrolase proenzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011622343"
FT   REGION          351..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ   SEQUENCE   563 AA;  59412 MW;  5392133B98EF2CD4 CRC64;
     MLKRFLPLAA LLSVTVSVPA LAQGVTSSAD PRATEAGREI LHEGGTAADA AIAMVAVLTL
     VEPQSSGIGG GGFMVHHNAK DGSISTIDGR EMAPASAKPD RFLGPDGKAR GYMDVIPGGL
     SVGVPGNVRL MEMAHKKWGK LEWKALFQPA IKLAEEGFIV TPALNNWLVQ FEPMWKEFPA
     PQAIYYVDGK PAPVGTRIKN PAYAKLLRDI AARGPDAFYT GANAKAISDA VAKAPRHPSQ
     LTVKDIAAYK AKERPAVCTT YRVYKVCGMG PPSSGATTVF GILGMIEGWD MKAMGKDNPM
     SWHLLSEAMQ LSYADRAAYL GDGDFVDVPV KGLLDKSYLA ERRQLISPFG AAGKYEPGTP
     PGAKPRAAAP PVQEQGTTHF VTADKDGNLV SMTSTIESIF GSQLMANGYF LNNELTDFDL
     APTEGGVPTA NRVEAGKRPL SSMSPTVVYG PDGKVILAVG SAGGKRIIMH VTKVLVGVLD
     WGLDAKTAME LPNLFFGQQG VLIENNEAGK AIAAKMKPFG YSFTATSLGS KLNAVERTAE
     GWRGAADPRG PGSSSIDGAP AQN
//
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