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ggt glutathione hydrolase proenzyme [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947947, updated on 17-Dec-2024

Summary

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Official Symbol
ggt
Official Full Name
glutathione hydrolase proenzyme
Primary source
ECOCYC:EG10374
Locus tag
b3447
See related
ASAP:ABE-0011257
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK3431
Summary
Small subunit is residues 26-390; large subunit is residues 391-580. [More information is available at EcoGene: EG10374]. The ggt gene encodes -glutamyltranspeptidase . [More information is available at EcoCyc: EG10374].
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Genomic context

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Sequence:
NC_000913.3 (3585081..3586823, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein YrhD Neighboring gene putative heat shock chaperone Neighboring gene DUF2756 domain-containing protein YhhA Neighboring gene glycerophosphodiester phosphodiesterase UgpQ Neighboring gene sn-glycerol 3-phosphate ABC transporter ATP binding subunit

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential. Suzuki H, et al. J Bacteriol, 1993 Sep. PMID 8104180, Free PMC Article
  2. gamma-Glutamyltranspeptidase and gamma-glutamyl peptide ligases: fluorophosphonate and phosphonodifluoromethyl ketone analogs as probes of tetrahedral transition state and gamma-glutamyl-phosphate intermediate. Hiratake J, et al. Methods Enzymol, 2002. PMID 12418234
  3. Autocatalytic processing of gamma-glutamyltranspeptidase. Suzuki H, et al. J Biol Chem, 2002 Nov 8. PMID 12207027
  4. Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial gamma-glutamyltranspeptidase. Suzuki H, et al. J Agric Food Chem, 2002 Jan 16. PMID 11782200
  5. [gamma-glutamyltranspeptidase: a new member of Ntn-hydrolase superfamily]. Suzuki H, et al. Tanpakushitsu Kakusan Koso, 2001 Sep. PMID 11552267

See all (42) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. beta-N-(gamma-L(+)-glutamyl)phenylhydrazine was prepared from L-glutamine and phenylhydrazine through a transpeptidation reaction of Escherichia coli gamma-glutamyltranspeptidase (although phenylhydrazine has been reported to be an inhibitor of the enzyme).
    Title: Enzymatic synthesis of β-N-(γ-L(+)-glutamyl)phenylhydrazine with Escherichia coli γ-glutamyltranspeptidase.
  2. the Ser463 residue contributes to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase
    Title: Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase.
  3. Data describe the crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin, and suggest a novel method for inhibition by glutamine antagonists.
    Title: Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists.
  4. N-terminus verified by Edman degradation on mature peptide
    Title: DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt.
  5. In contrast to the human GGT1, the E. coli enzyme was a nonselective enzyme that accommodated substrates without specifically recognizing the C-terminal carboxy group of the Cys-Gly moiety
    Title: Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase.
  6. crystal structure
    Title: Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables acyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables gamma-glutamyl-peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables glutathione hydrolase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables glutathione hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables leukotriene C4 gamma-glutamyl transferase activity IEA
Inferred from Electronic Annotation
more info
  
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within amino acid salvage IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in glutathione biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in glutathione catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in glutathione metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within self proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
glutathione hydrolase proenzyme
NP_417904.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    3585081..3586823 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417904.1 glutathione hydrolase proenzyme [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417904.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7TID5
    Conserved Domains (1) summary
    PRK09615
    Location:1 → 580
    ggt; gamma-glutamyltranspeptidase; Reviewed
Nucleotide Protein
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