ID A0A1B9YSH1_9BRAD Unreviewed; 581 AA.
AC A0A1B9YSH1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=LMTR3_00305 {ECO:0000313|EMBL:OCK57593.1};
OS Bradyrhizobium sp. LMTR 3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK57593.1, ECO:0000313|Proteomes:UP000093220};
RN [1] {ECO:0000313|EMBL:OCK57593.1, ECO:0000313|Proteomes:UP000093220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK57593.1,
RC ECO:0000313|Proteomes:UP000093220};
RA Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA Martinez E.;
RL Submitted (JUL-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}.
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:OCK57593.1}.
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DR EMBL; MAXC01000023; OCK57593.1; -; Genomic_DNA.
DR RefSeq; WP_065746287.1; NZ_MAXC01000023.1.
DR AlphaFoldDB; A0A1B9YSH1; -.
DR STRING; 189873.LMTR3_00305; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000093220; 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 Reference proteome {ECO:0000313|Proteomes:UP000093220};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..581
FT /note="Glutathione hydrolase proenzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008641085"
FT REGION 557..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 581 AA; 60843 MW; EBE7E51774AD5B8D CRC64;
MTIFQISRRK AIAAIALIFA CGTTAFAQDR RGFHSSLDLS AVRSIPAEHG MVVAQEKIAA
EVGADILRQG GNAIDAAVAT GFALAVTYPR AGNIGGGGFM VIHSAERNED VTIDYRETAP
AATTRDIFLG PDGKPDTDKS RNSALGIGVP GTVAGLALAL EKYGSGRFTL AQVLKPAIEL
ARDGFVIADD TADTLPDLYR RMARWPNPAK AFSRDDGTAL REGDRLAQAD LAATLSAIAE
QGPRGFYQGP VAERLAKAVR DAGGIMTADD LKSYEAVIRS PVRGSYRGYE IVSMPLPSSG
GTVLLETLNI LEGFAMADMK QGSAPSLHVM IEAMKRAYAD RARYLGDPAF VNAPANILIA
KDYAAKQRAS IDLARATPAD ALSASLPREG SNTTHYSVVD AGGNAVSNTY TLNFSYGVGL
VADGTGVLLN NELDDFTAAP GAANAFGLVG FEANLPGPGK RPLSSMSPTI VLKDGKPALV
TGSPGGSRII SAVLQVVVNA LDYKMDVATA VAAPRLHHQW MPDVVRVERG FPQETLDALK
EKGHQVIEPL GQTSANSIAV TPSGLRGAPD PRTRGAAAVG H
//
