ID A0A0D5NIR5_9BACL Unreviewed; 535 AA.
AC A0A0D5NIR5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, 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=VN24_11840 {ECO:0000313|EMBL:AJY75146.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY75146.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY75146.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY75146.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-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|RuleBase:RU368036}.
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DR EMBL; CP011058; AJY75146.1; -; Genomic_DNA.
DR RefSeq; WP_045670579.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NIR5; -.
DR STRING; 1126833.VN24_11840; -.
DR KEGG; pbj:VN24_11840; -.
DR PATRIC; fig|1126833.4.peg.2590; -.
DR HOGENOM; CLU_014813_3_2_9; -.
DR OrthoDB; 9781342at2; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000032633; 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; 1.10.246.230; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000032633};
KW Transferase {ECO:0000256|RuleBase:RU368036};
KW Zymogen {ECO:0000256|RuleBase:RU368036}.
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600101-1"
SQ SEQUENCE 535 AA; 57419 MW; 70374E218305F99D CRC64;
MFDRPSGYRQ QTRSVIHAAR GMVATSQPLA SAAGIEILQS GGNAFDAAVA VAAVLCVVEP
MMTGLGGDMF ALVHDGKTGT IEGLNASGRS AAMASVEAYR SMGYEQIPDH GPLSVSVPGV
VDGWAQLLAK YGTMSFKEVL APAIRYAENG FPVSEMVAYY WSKAEPLLRK SAEASRKYLM
NGKAPAEGTL FKQPDLAATL KLLAEQGKNA FYQGKIADQI EAFMIREGGL LRKSDFASHQ
SDWVEPISTT YRGHSILEIP PNGQGLVVLE MLNILEQFDV ASMGHNSADY IRLFAEAKKL
AYADRDRYIA DSDFAELPVD RLLSKEYAAE LADRIRNSAS VAAPPGIELG GDTVYLTVVD
HEGNIASVVN SVFSLFGSGE LVEDTGIFLQ NRGSLFSLHP SHVNAVAPRK RPFHTIIPSL
VLKNGKPLVS FGVMGADMQP QGQVQVLVNM IDFGMNIQEA GEAPRFRHYN DGLYLETGIG
EETSRELAGI GYTILQPGDG DAFGVGGYQG IRIDPDTGVL QGGSDPRKDG CAIGF
//
