ECOLI:GSH1

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	gshA (synonyms: gsh-I)
Protein Name(s)	Glutamate--cysteine ligase Gamma-ECS GCS Gamma-glutamylcysteine synthetase
External Links
UniProt	P0A6W9
EMBL	X03954 U00096 AP009048
PIR	A65049
RefSeq	NP_417173.1 YP_490902.1
PDB	1V4G 1VA6 2D32 2D33
PDBsum	1V4G 1VA6 2D32 2D33
ProteinModelPortal	P0A6W9
SMR	P0A6W9
DIP	DIP-48212N
IntAct	P0A6W9
STRING	511145.b2688
PaxDb	P0A6W9
PRIDE	P0A6W9
DNASU	944881
EnsemblBacteria	AAC75735 BAA16555
GeneID	12933277 944881
KEGG	ecj:Y75_p2631 eco:b2688
PATRIC	32120770
EchoBASE	EB0413
EcoGene	EG10418
eggNOG	COG2918
HOGENOM	HOG000266224
InParanoid	P0A6W9
KO	K01919
OMA	QTISGIH
OrthoDB	EOG6BKJ7H
PhylomeDB	P0A6W9
BioCyc	EcoCyc:GLUTCYSLIG-MONOMER ECOL316407:JW2663-MONOMER MetaCyc:GLUTCYSLIG-MONOMER
BRENDA	6.3.2.2
SABIO-RK	P0A6W9
UniPathway	UPA00142
EvolutionaryTrace	P0A6W9
PRO	PR:P0A6W9
Proteomes	UP000000318 UP000000625
Genevestigator	P0A6W9
GO	GO:0005524 GO:0004357 GO:0046872 GO:0071243 GO:0071288 GO:0006750 GO:0006972
HAMAP	MF_00578
InterPro	IPR007370 IPR006334
Pfam	PF04262
TIGRFAMs	TIGR01434

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0046872	metal ion binding	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10418 PANTHER:PTN002215154	F	Seeded From UniProt	complete
involved_in	GO:0006750	glutathione biosynthetic process	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10418 PANTHER:PTN002215154	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10418 PANTHER:PTN002215154	C	Seeded From UniProt	complete
enables	GO:0004357	glutamate-cysteine ligase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10418 PANTHER:PTN002215154	F	Seeded From UniProt	complete
involved_in	GO:0071288	cellular response to mercury ion	PMID:9439611^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0071243	cellular response to arsenic-containing substance	PMID:9439611^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	PMID:11675389^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006972	hyperosmotic response	PMID:1972940^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006750	glutathione biosynthetic process	PMID:1096956^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004357	glutamate-cysteine ligase activity	PMID:2895925^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR014746	F	Seeded From UniProt	complete
enables	GO:0004357	glutamate-cysteine ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006334 InterPro:IPR007370	F	Seeded From UniProt	complete
involved_in	GO:0006750	glutathione biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006334 InterPro:IPR007370	P	Seeded From UniProt	complete
enables	GO:0004357	glutamate-cysteine ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.3.2.2	F	Seeded From UniProt	complete
enables	GO:0004357	glutamate-cysteine ligase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000030623	F	Seeded From UniProt	complete
involved_in	GO:0006750	glutathione biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000030623	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0006750	glutathione biosynthetic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0317 UniPathway:UPA00142	P	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^2.0 ^2.1 Latinwo, LM et al. (1998) Effects of intracellular glutathione on sensitivity of Escherichia coli to mercury and arsenite. Biochem. Biophys. Res. Commun. 242 67-70 PubMed GONUTS page
↑ Kelly, BS et al. (2002) Escherichia coli gamma-glutamylcysteine synthetase. Two active site metal ions affect substrate and inhibitor binding. J. Biol. Chem. 277 50-8 PubMed GONUTS page
↑ McLaggan, D et al. (1990) Involvement of gamma-glutamyl peptides in osmoadaptation of Escherichia coli. J. Bacteriol. 172 3631-6 PubMed GONUTS page
↑ Apontoweil, P & Berends, W (1975) Isolation and initial characterization of glutathione-deficient mutants of Escherichia coli K 12. Biochim. Biophys. Acta 399 10-22 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Huang, CS et al. (1988) On the active site thiol of gamma-glutamylcysteine synthetase: relationships to catalysis, inhibition, and regulation. Proc. Natl. Acad. Sci. U.S.A. 85 2464-8 PubMed GONUTS page

[PMID:21873635-1] 1.0 ^1.1 ^1.2 ^1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:9439611-2] 2.0 ^2.1 Latinwo, LM et al. (1998) Effects of intracellular glutathione on sensitivity of Escherichia coli to mercury and arsenite. Biochem. Biophys. Res. Commun. 242 67-70 PubMed GONUTS page

[PMID:11675389-3] Kelly, BS et al. (2002) Escherichia coli gamma-glutamylcysteine synthetase. Two active site metal ions affect substrate and inhibitor binding. J. Biol. Chem. 277 50-8 PubMed GONUTS page

[PMID:1972940-4] McLaggan, D et al. (1990) Involvement of gamma-glutamyl peptides in osmoadaptation of Escherichia coli. J. Bacteriol. 172 3631-6 PubMed GONUTS page

[PMID:1096956-5] Apontoweil, P & Berends, W (1975) Isolation and initial characterization of glutathione-deficient mutants of Escherichia coli K 12. Biochim. Biophys. Acta 399 10-22 PubMed GONUTS page

[PMID:18304323-6] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:2895925-7] Huang, CS et al. (1988) On the active site thiol of gamma-glutamylcysteine synthetase: relationships to catalysis, inhibition, and regulation. Proc. Natl. Acad. Sci. U.S.A. 85 2464-8 PubMed GONUTS page

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ECOLI:GSH1

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