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ECOLI:GGT

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ggt
Protein Name(s) Glutathione hydrolase proenzyme

Gamma-glutamyltranspeptidase proenzyme (ECO:0000303 with PMID:2570061[1]) GGT Glutathione hydrolase large chain Glutathione hydrolase small chain

External Links
UniProt P18956
EMBL M28722
U18997
U00096
AP009048
U00039
PIR JV0028
RefSeq NP_417904.1
WP_000595082.1
PDB 2DBU
2DBW
2DBX
2DG5
2E0W
2E0X
2E0Y
2Z8I
2Z8J
2Z8K
5B5T
PDBsum 2DBU
2DBW
2DBX
2DG5
2E0W
2E0X
2E0Y
2Z8I
2Z8J
2Z8K
5B5T
ProteinModelPortal P18956
SMR P18956
BioGrid 4261666
DIP DIP-9758N
IntAct P18956
STRING 316385.ECDH10B_3621
MEROPS T03.001
PaxDb P18956
PRIDE P18956
EnsemblBacteria AAC76472
BAE77846
GeneID 947947
KEGG ecj:JW3412
eco:b3447
PATRIC fig|511145.12.peg.3544
EchoBASE EB0369
EcoGene EG10374
eggNOG ENOG4105CFB
COG0405
HOGENOM HOG000175617
InParanoid P18956
KO K00681
PhylomeDB P18956
BioCyc EcoCyc:EG10374-MONOMER
MetaCyc:EG10374-MONOMER
BRENDA 2.3.2.2
3.4.19.13
SABIO-RK P18956
UniPathway UPA00204
EvolutionaryTrace P18956
PRO PR:P18956
Proteomes UP000000318
UP000000625
GO GO:0030288
GO:0042597
GO:0036374
GO:0102953
GO:0103068
GO:0043102
GO:0006750
GO:0006751
GO:0097264
InterPro IPR000101
IPR029055
SUPFAM SSF56235
TIGRFAMs TIGR00066
PROSITE PS00462

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0042597

periplasmic space

PMID:2877975[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0097264

self proteolysis

PMID:10869181[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043102

amino acid salvage

PMID:8104180[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0036374

glutathione hydrolase activity

PMID:2877974[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0034722

gamma-glutamyl-peptidase activity

PMID:2877974[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0030288

outer membrane-bounded periplasmic space

PMID:2877975[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006751

glutathione catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000101

P

Seeded From UniProt

complete

enables

GO:0036374

glutathione hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000101

F

Seeded From UniProt

complete

enables

GO:0036374

glutathione hydrolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.19.13

F

Seeded From UniProt

complete

enables

GO:0102953

hypoglycin A gamma-glutamyl transpeptidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.2.2

F

Seeded From UniProt

complete

enables

GO:0103068

leukotriene C4 gamma-glutamyl transferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.2.2

F

Seeded From UniProt

complete

part_of

GO:0042597

periplasmic space

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0574
UniProtKB-SubCell:SL-0200

C

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0006750

glutathione biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0317

P

Seeded From UniProt

complete

involved_in

GO:0006749

glutathione metabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00204

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Suzuki, H et al. (1989) DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt. J. Bacteriol. 171 5169-72 PubMed GONUTS page
  2. 2.0 2.1 Suzuki, H et al. (1986) gamma-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. J. Bacteriol. 168 1332-5 PubMed GONUTS page
  3. Inoue, M et al. (2000) Identification of catalytic nucleophile of Escherichia coli gamma-glutamyltranspeptidase by gamma-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile. Biochemistry 39 7764-71 PubMed GONUTS page
  4. Suzuki, H et al. (1993) Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential. J. Bacteriol. 175 6038-40 PubMed GONUTS page
  5. 5.0 5.1 Suzuki, H et al. (1986) gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties. J. Bacteriol. 168 1325-31 PubMed GONUTS page