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Protein

Gamma-glutamyltranspeptidase

Gene

ggt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.1 Publication
Glutathione + H2O = L-cysteinylglycine + L-glutamate.By similarity

Pathwayi: glutathione metabolism

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei114 – 1141Glutamate1 Publication
Active sitei391 – 3911Nucleophile2 Publications
Binding sitei409 – 4091Glutamate1 Publication
Binding sitei411 – 4111Glutamate1 Publication
Binding sitei430 – 4301Glutamate1 Publication
Binding sitei433 – 4331Glutamate1 Publication

GO - Molecular functioni

  • gamma-glutamyltransferase activity Source: EcoliWiki
  • glutathione hydrolase activity Source: UniProtKB-EC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG10374-MONOMER.
ECOL316407:JW3412-MONOMER.
MetaCyc:EG10374-MONOMER.
RETL1328306-WGS:GSTH-3604-MONOMER.
BRENDAi2.3.2.2. 2026.
3.4.19.13. 2026.
SABIO-RKP18956.
UniPathwayiUPA00204.

Protein family/group databases

MEROPSiT03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltranspeptidase1 Publication (EC:2.3.2.22 Publications)
Alternative name(s):
Glutathione hydrolase (EC:3.4.19.13By similarity)
Cleaved into the following 2 chains:
Gene namesi
Name:ggt
Ordered Locus Names:b3447, JW3412
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10374. ggt.

Subcellular locationi

GO - Cellular componenti

  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi391 – 3911T → A: Abolishes autocatalytic cleavage. 1 Publication
Mutagenesisi513 – 5131R → A: Not processed into its subunits. 1 Publication
Mutagenesisi571 – 5711R → G: Not processed into its subunits. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 390365Gamma-glutamyltranspeptidase large chainPRO_0000011052Add
BLAST
Chaini391 – 580190Gamma-glutamyltranspeptidase small chainPRO_0000011053Add
BLAST

Post-translational modificationi

Cleaved by autocatalysis into a large and a small subunit.

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP18956.

Interactioni

Subunit structurei

This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide.4 Publications

Protein-protein interaction databases

BioGridi4261666. 368 interactions.
DIPiDIP-9758N.
IntActiP18956. 1 interaction.
MINTiMINT-1260227.
STRINGi511145.b3447.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 413Combined sources
Beta strandi44 – 485Combined sources
Beta strandi50 – 545Combined sources
Helixi56 – 6712Combined sources
Helixi72 – 8615Combined sources
Turni88 – 903Combined sources
Beta strandi93 – 10210Combined sources
Beta strandi108 – 1136Combined sources
Turni123 – 1264Combined sources
Beta strandi129 – 1313Combined sources
Helixi135 – 1395Combined sources
Helixi142 – 1443Combined sources
Helixi150 – 16112Combined sources
Helixi166 – 17914Combined sources
Helixi185 – 1939Combined sources
Helixi195 – 1973Combined sources
Helixi199 – 2013Combined sources
Helixi203 – 2097Combined sources
Helixi225 – 23713Combined sources
Helixi240 – 2434Combined sources
Helixi246 – 25712Combined sources
Helixi264 – 2696Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi278 – 2825Combined sources
Beta strandi285 – 2895Combined sources
Helixi296 – 30712Combined sources
Helixi312 – 3154Combined sources
Helixi320 – 34021Combined sources
Turni344 – 3463Combined sources
Helixi351 – 3544Combined sources
Helixi357 – 3648Combined sources
Helixi375 – 3773Combined sources
Helixi384 – 3863Combined sources
Beta strandi392 – 3976Combined sources
Beta strandi403 – 4097Combined sources
Turni413 – 4164Combined sources
Helixi421 – 4233Combined sources
Helixi430 – 4334Combined sources
Beta strandi434 – 4374Combined sources
Beta strandi467 – 4715Combined sources
Beta strandi474 – 4796Combined sources
Helixi484 – 4863Combined sources
Helixi487 – 49913Combined sources
Helixi505 – 5106Combined sources
Beta strandi518 – 5203Combined sources
Beta strandi523 – 5253Combined sources
Helixi531 – 5399Combined sources
Beta strandi544 – 5463Combined sources
Beta strandi554 – 5585Combined sources
Beta strandi564 – 5685Combined sources
Beta strandi576 – 5794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBUX-ray1.95A/C25-390[»]
B/D391-580[»]
2DBWX-ray1.80A/C25-390[»]
B/D391-580[»]
2DBXX-ray1.70A/C25-390[»]
B/D391-580[»]
2DG5X-ray1.60A/C25-390[»]
B/D391-580[»]
2E0WX-ray2.55A/B25-580[»]
2E0XX-ray1.95A/C25-390[»]
B/D391-580[»]
2E0YX-ray2.02A/C25-390[»]
B/D391-580[»]
2Z8IX-ray1.65A/C25-390[»]
B/D391-580[»]
2Z8JX-ray2.05A/C25-390[»]
B/D391-580[»]
2Z8KX-ray1.65A/C25-390[»]
B/D391-580[»]
ProteinModelPortaliP18956.
SMRiP18956. Positions 29-580.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18956.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni462 – 4632Glutamate binding
Regioni483 – 4842Glutamate binding

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105CFB. Bacteria.
COG0405. LUCA.
HOGENOMiHOG000175617.
InParanoidiP18956.
KOiK00681.
OMAiSTSHFVI.
OrthoDBiEOG62K1RV.
PhylomeDBiP18956.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18956-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:580
Mass (Da):61,768
Last modified:November 1, 1990 - v1
Checksum:i772F652EBA2A5F00
GO

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.
PIRiJV0028. EKECEX.
RefSeqiNP_417904.1. NC_000913.3.
WP_000595082.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76472; AAC76472; b3447.
BAE77846; BAE77846; BAE77846.
GeneIDi947947.
KEGGiecj:JW3412.
eco:b3447.
PATRICi32122334. VBIEscCol129921_3544.

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.
PIRiJV0028. EKECEX.
RefSeqiNP_417904.1. NC_000913.3.
WP_000595082.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBUX-ray1.95A/C25-390[»]
B/D391-580[»]
2DBWX-ray1.80A/C25-390[»]
B/D391-580[»]
2DBXX-ray1.70A/C25-390[»]
B/D391-580[»]
2DG5X-ray1.60A/C25-390[»]
B/D391-580[»]
2E0WX-ray2.55A/B25-580[»]
2E0XX-ray1.95A/C25-390[»]
B/D391-580[»]
2E0YX-ray2.02A/C25-390[»]
B/D391-580[»]
2Z8IX-ray1.65A/C25-390[»]
B/D391-580[»]
2Z8JX-ray2.05A/C25-390[»]
B/D391-580[»]
2Z8KX-ray1.65A/C25-390[»]
B/D391-580[»]
ProteinModelPortaliP18956.
SMRiP18956. Positions 29-580.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261666. 368 interactions.
DIPiDIP-9758N.
IntActiP18956. 1 interaction.
MINTiMINT-1260227.
STRINGi511145.b3447.

Protein family/group databases

MEROPSiT03.001.

Proteomic databases

PaxDbiP18956.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76472; AAC76472; b3447.
BAE77846; BAE77846; BAE77846.
GeneIDi947947.
KEGGiecj:JW3412.
eco:b3447.
PATRICi32122334. VBIEscCol129921_3544.

Organism-specific databases

EchoBASEiEB0369.
EcoGeneiEG10374. ggt.

Phylogenomic databases

eggNOGiENOG4105CFB. Bacteria.
COG0405. LUCA.
HOGENOMiHOG000175617.
InParanoidiP18956.
KOiK00681.
OMAiSTSHFVI.
OrthoDBiEOG62K1RV.
PhylomeDBiP18956.

Enzyme and pathway databases

UniPathwayiUPA00204.
BioCyciEcoCyc:EG10374-MONOMER.
ECOL316407:JW3412-MONOMER.
MetaCyc:EG10374-MONOMER.
RETL1328306-WGS:GSTH-3604-MONOMER.
BRENDAi2.3.2.2. 2026.
3.4.19.13. 2026.
SABIO-RKP18956.

Miscellaneous databases

EvolutionaryTraceiP18956.
PROiP18956.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt."
    Suzuki H., Kumagai H., Echigo T., Tochikura T.
    J. Bacteriol. 171:5169-5172(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41 AND 391-403.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-362.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Escherichia coli gamma-glutamyltranspeptidase mutants deficient in processing to subunits."
    Hashimoto W., Suzuki H., Nohara S., Kumagai H.
    Biochem. Biophys. Res. Commun. 189:173-178(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ARG-513 AND ARG-571, AUTOCATALYTIC CLEAVAGE.
  6. "Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate."
    Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.
    Proc. Natl. Acad. Sci. U.S.A. 103:6471-6476(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-580 IN COMPLEX WITH GLUTAMATE, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AUTOCATALYTIC CLEAVAGE.
  7. "Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism."
    Okada T., Suzuki H., Wada K., Kumagai H., Fukuyama K.
    J. Biol. Chem. 282:2433-2439(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-580 OF MUTANT ALA-391, SUBUNIT, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF THR-391.
  8. "Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists."
    Wada K., Hiratake J., Irie M., Okada T., Yamada C., Kumagai H., Suzuki H., Fukuyama K.
    J. Mol. Biol. 380:361-372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 25-580 IN COMPLEXES WITH AZASERINE AND ACIVICIN, ACTIVE SITE, SUBUNIT, AUTOCATALYTIC CLEAVAGE.

Entry informationi

Entry nameiGGT_ECOLI
AccessioniPrimary (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: January 20, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.