GenomeNet

Database: UniProt
Entry: J3CV65_9BURK
LinkDB: J3CV65_9BURK
Original site: J3CV65_9BURK 
ID   J3CV65_9BURK            Unreviewed;       578 AA.
AC   J3CV65;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=PMI12_00843 {ECO:0000313|EMBL:EJL79154.1};
OS   Variovorax sp. CF313.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL79154.1, ECO:0000313|Proteomes:UP000007277};
RN   [1] {ECO:0000313|EMBL:EJL79154.1, ECO:0000313|Proteomes:UP000007277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF313 {ECO:0000313|EMBL:EJL79154.1,
RC   ECO:0000313|Proteomes:UP000007277};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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}.
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:EJL79154.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AKIW01000013; EJL79154.1; -; Genomic_DNA.
DR   RefSeq; WP_007829388.1; NZ_AKIW01000013.1.
DR   AlphaFoldDB; J3CV65; -.
DR   MEROPS; T03.001; -.
DR   PATRIC; fig|1144315.3.peg.829; -.
DR   UniPathway; UPA00204; -.
DR   Proteomes; UP000007277; 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.
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   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368036};
KW   Zymogen {ECO:0000256|RuleBase:RU368036}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..578
FT                   /note="Glutathione hydrolase proenzyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003764769"
FT   ACT_SITE        379
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ   SEQUENCE   578 AA;  61255 MW;  07F8CF0407E64299 CRC64;
     MQQIQWTPKL RAAVAAVLAL AAAGASNAAS VAPVASEHGM VVSAQHLASK VGVDVLKRGG
     NAVDAAVAVG YALAVVYPAA GNLGGGGFMT VQLADGRKTF LDFREKAPLA ATANMYLDKD
     GNVIKGLSTN GHLAVGVPGS VSGMEYAREK YGTMKRADLI APSIQLADKG FALEQGDIDM
     LLTATNDFKK DPVSGAIFLN KGEPFAVGQK LVQKDLARTL KEISAKGTDG FYKGWVGQAI
     VASSQAGKGI ITQADLDQYK TRELAPVECD YRGYRVVSAP PPSSGGVIIC EMLNILEGYP
     LKDLGFRSAQ SVHYQIEAMR HAYVDRNSYL GDPDFVKNPL ERLLDKGYAE KIRAVIDPKK
     AGVSKDIKPG VAPHEGSNTT HYSITDQWGN AVSVTYTLND WFGAKVTAAK TGVLLNNEMD
     DFTAKVGVPN LYGLVQGEAN KIEPGKRPLS SMSPTIVSKD GKPVFVVGTP GGSRIITAVL
     HTILNVVDYG MNVQEAVDAP RFHQQWLPDV TNVETFALSP DTRKILTDMG HNLGVPQPAN
     HLAAIIVGAP SLGGKPVGAN RFYGANDPRR NTGLAAGY
//
DBGET integrated database retrieval system