UniProtKB - P18956 (GGT_ECOLI)
Protein
Glutathione hydrolase proenzyme
Gene
ggt
Organism
Escherichia coli (strain K12)
Status
Functioni
Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D-gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acceptors (PubMed:2877974). The KM values for gamma-glutamyl acceptors are so high that it has been proposed transpeptidation is not the physiological role in E.coli (PubMed:2877974, PubMed:8104180).1 Publication1 Publication
Catalytic activityi
- an α-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-α-aminoacyl-[peptide]1 PublicationEC:2.3.2.21 Publication
- EC:3.4.19.131 Publication
- EC:3.4.19.131 Publication
Activity regulationi
Transferase and hydrolase activities are inhibited by L-Ala and L-Gln, and also by GGT affinity labeling reagents such as azaserine and 6-diazo-5-oxo-nor-leucine.1 Publication
Kineticsi
- KM=35 µM for glutathione transfer to glycylglycine (gly-gly)1 Publication
- KM=35 µM for gamma-glutamyl-p-nitroanilide (gamma-GpNA) transfer to gly-gly1 Publication
- KM=29 µM for glutathione hydrolysis1 Publication
- KM=68 µM for gamma-GpNA hydrolysis1 Publication
pH dependencei
Optimum pH is 8.73 for transfer of p-nitroanilide from gamma-GpNA to gly-gly and 9.25 for hydrolysis of gamma-GpNA.1 Publication
Temperature dependencei
Optimum temperature is 50 degrees Celsius for both transferase and hydrolase activities.1 Publication
: glutathione metabolism Pathwayi
This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 114 | Glutamate1 Publication | 1 | |
Active sitei | 391 | Nucleophile2 Publications | 1 | |
Binding sitei | 409 | Glutamate1 Publication | 1 | |
Binding sitei | 411 | Glutamate1 Publication | 1 | |
Binding sitei | 430 | Glutamate1 Publication | 1 | |
Binding sitei | 433 | Glutamate1 Publication | 1 |
GO - Molecular functioni
- gamma-glutamyl-peptidase activity Source: EcoCyc
- glutathione hydrolase activity Source: EcoCyc
- hypoglycin A gamma-glutamyl transpeptidase activity Source: UniProtKB-EC
- leukotriene C4 gamma-glutamyl transferase activity Source: UniProtKB-EC
GO - Biological processi
- amino acid salvage Source: EcoCyc
- glutathione biosynthetic process Source: UniProtKB-KW
- glutathione catabolic process Source: InterPro
- self proteolysis Source: EcoCyc
Keywordsi
Molecular function | Acyltransferase, Hydrolase, Protease, Transferase |
Biological process | Glutathione biosynthesis |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10374-MONOMER MetaCyc:EG10374-MONOMER |
BRENDAi | 2.3.2.2, 2026 3.4.19.13, 2026 |
SABIO-RKi | P18956 |
UniPathwayi | UPA00204 |
Protein family/group databases
MEROPSi | T03.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Glutathione hydrolase proenzyme (EC:3.4.19.131 Publication)Alternative name(s): Cleaved into the following 2 chains: |
Gene namesi | Name:ggt Ordered Locus Names:b3447, JW3412 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- Periplasm 2 Publications
Other locations
- outer membrane-bounded periplasmic space Source: EcoCyc
- periplasmic space Source: EcoliWiki
Keywords - Cellular componenti
PeriplasmPathology & Biotechi
Disruption phenotypei
Loss of growth using exogenous gamma-glutamyl peptides as amino acid sources.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 391 | T → A: Abolishes autocatalytic cleavage, loss of enzymatic activity. 1 Publication | 1 | |
Mutagenesisi | 513 | R → A: Not processed into its subunits, loss of enzymatic activity. 1 Publication | 1 | |
Mutagenesisi | 571 | R → G: Not processed into its subunits, loss of enzymatic activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | 1 PublicationAdd BLAST | 25 | |
ChainiPRO_0000011052 | 26 – 390 | Glutathione hydrolase large chainAdd BLAST | 365 | |
ChainiPRO_0000011053 | 391 – 580 | Glutathione hydrolase small chainAdd BLAST | 190 |
Post-translational modificationi
Cleaved by autocatalysis into a large and a small subunit.5 Publications
Keywords - PTMi
ZymogenProteomic databases
jPOSTi | P18956 |
PaxDbi | P18956 |
PRIDEi | P18956 |
Interactioni
Subunit structurei
This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.
5 PublicationsProtein-protein interaction databases
BioGRIDi | 4261666, 434 interactors |
DIPi | DIP-9758N |
IntActi | P18956, 1 interactor |
STRINGi | 511145.b3447 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P18956 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P18956 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 462 – 463 | Glutamate binding | 2 | |
Regioni | 483 – 484 | Glutamate binding | 2 |
Sequence similaritiesi
Belongs to the gamma-glutamyltransferase family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | COG0405, Bacteria |
HOGENOMi | CLU_014813_0_3_6 |
InParanoidi | P18956 |
PhylomeDBi | P18956 |
Family and domain databases
Gene3Di | 1.10.246.130, 1 hit 3.60.20.40, 1 hit |
InterProi | View protein in InterPro IPR043138, GGT_lsub_C IPR000101, GGT_peptidase IPR043137, GGT_ssub IPR029055, Ntn_hydrolases_N |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR00066, g_glut_trans, 1 hit |
PROSITEi | View protein in PROSITE PS00462, G_GLU_TRANSPEPTIDASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P18956-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MIKPTFLRRV AIAALLSGSC FSAAAAPPAP PVSYGVEEDV FHPVRAKQGM
60 70 80 90 100
VASVDATATQ VGVDILKEGG NAVDAAVAVG YALAVTHPQA GNLGGGGFML
110 120 130 140 150
IRSKNGNTTA IDFREMAPAK ATRDMFLDDQ GNPDSKKSLT SHLASGTPGT
160 170 180 190 200
VAGFSLALDK YGTMPLNKVV QPAFKLARDG FIVNDALADD LKTYGSEVLP
210 220 230 240 250
NHENSKAIFW KEGEPLKKGD TLVQANLAKS LEMIAENGPD EFYKGTIAEQ
260 270 280 290 300
IAQEMQKNGG LITKEDLAAY KAVERTPISG DYRGYQVYSM PPPSSGGIHI
310 320 330 340 350
VQILNILENF DMKKYGFGSA DAMQIMAEAE KYAYADRSEY LGDPDFVKVP
360 370 380 390 400
WQALTNKAYA KSIADQIDIN KAKPSSEIRP GKLAPYESNQ TTHYSVVDKD
410 420 430 440 450
GNAVAVTYTL NTTFGTGIVA GESGILLNNQ MDDFSAKPGV PNVYGLVGGD
460 470 480 490 500
ANAVGPNKRP LSSMSPTIVV KDGKTWLVTG SPGGSRIITT VLQMVVNSID
510 520 530 540 550
YGLNVAEATN APRFHHQWLP DELRVEKGFS PDTLKLLEAK GQKVALKEAM
560 570 580
GSTQSIMVGP DGELYGASDP RSVDDLTAGY
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M28722 Genomic DNA Translation: AAA23869.1 U18997 Genomic DNA Translation: AAA58245.1 U00096 Genomic DNA Translation: AAC76472.1 AP009048 Genomic DNA Translation: BAE77846.1 U00039 Genomic DNA Translation: AAB18422.1 |
PIRi | JV0028, EKECEX |
RefSeqi | NP_417904.1, NC_000913.3 WP_000595082.1, NZ_SSZK01000008.1 |
Genome annotation databases
EnsemblBacteriai | AAC76472; AAC76472; b3447 BAE77846; BAE77846; BAE77846 |
GeneIDi | 947947 |
KEGGi | ecj:JW3412 eco:b3447 |
PATRICi | fig|511145.12.peg.3544 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M28722 Genomic DNA Translation: AAA23869.1 U18997 Genomic DNA Translation: AAA58245.1 U00096 Genomic DNA Translation: AAC76472.1 AP009048 Genomic DNA Translation: BAE77846.1 U00039 Genomic DNA Translation: AAB18422.1 |
PIRi | JV0028, EKECEX |
RefSeqi | NP_417904.1, NC_000913.3 WP_000595082.1, NZ_SSZK01000008.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2DBU | X-ray | 1.95 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2DBW | X-ray | 1.80 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2DBX | X-ray | 1.70 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2DG5 | X-ray | 1.60 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2E0W | X-ray | 2.55 | A/B | 25-580 | [»] | |
2E0X | X-ray | 1.95 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2E0Y | X-ray | 2.02 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2Z8I | X-ray | 1.65 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2Z8J | X-ray | 2.05 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
2Z8K | X-ray | 1.65 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
5B5T | X-ray | 1.70 | A/C | 25-390 | [»] | |
B/D | 391-580 | [»] | ||||
SMRi | P18956 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261666, 434 interactors |
DIPi | DIP-9758N |
IntActi | P18956, 1 interactor |
STRINGi | 511145.b3447 |
Protein family/group databases
MEROPSi | T03.001 |
Proteomic databases
jPOSTi | P18956 |
PaxDbi | P18956 |
PRIDEi | P18956 |
Genome annotation databases
EnsemblBacteriai | AAC76472; AAC76472; b3447 BAE77846; BAE77846; BAE77846 |
GeneIDi | 947947 |
KEGGi | ecj:JW3412 eco:b3447 |
PATRICi | fig|511145.12.peg.3544 |
Organism-specific databases
EchoBASEi | EB0369 |
Phylogenomic databases
eggNOGi | COG0405, Bacteria |
HOGENOMi | CLU_014813_0_3_6 |
InParanoidi | P18956 |
PhylomeDBi | P18956 |
Enzyme and pathway databases
UniPathwayi | UPA00204 |
BioCyci | EcoCyc:EG10374-MONOMER MetaCyc:EG10374-MONOMER |
BRENDAi | 2.3.2.2, 2026 3.4.19.13, 2026 |
SABIO-RKi | P18956 |
Miscellaneous databases
EvolutionaryTracei | P18956 |
PROi | PR:P18956 |
Family and domain databases
Gene3Di | 1.10.246.130, 1 hit 3.60.20.40, 1 hit |
InterProi | View protein in InterPro IPR043138, GGT_lsub_C IPR000101, GGT_peptidase IPR043137, GGT_ssub IPR029055, Ntn_hydrolases_N |
SUPFAMi | SSF56235, SSF56235, 1 hit |
TIGRFAMsi | TIGR00066, g_glut_trans, 1 hit |
PROSITEi | View protein in PROSITE PS00462, G_GLU_TRANSPEPTIDASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GGT_ECOLI | |
Accessioni | P18956Primary (citable) accession number: P18956 Secondary accession number(s): Q2M7B0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1990 |
Last sequence update: | November 1, 1990 | |
Last modified: | April 7, 2021 | |
This is version 176 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families