ECOLI:GLNA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	glnA
Protein Name(s)	Glutamine synthetase Glutamate--ammonia ligase
External Links
UniProt	P0A9C5
EMBL	X05173 M13746 L19201 U00096 AP009048 J01618 M10421 K02176
PIR	S40815
RefSeq	NP_418306.1 YP_491580.1
ProteinModelPortal	P0A9C5
SMR	P0A9C5
DIP	DIP-9777N
IntAct	P0A9C5
STRING	511145.b3870
BindingDB	P0A9C5
ChEMBL	CHEMBL3789
SWISS-2DPAGE	P0A9C5
PaxDb	P0A9C5
PRIDE	P0A9C5
EnsemblBacteria	AAC76867 BAE77439
GeneID	12933636 948370
KEGG	ecj:Y75_p3316 eco:b3870
PATRIC	32123243
EchoBASE	EB0378
EcoGene	EG10383
eggNOG	COG0174
HOGENOM	HOG000005157
InParanoid	P0A9C5
KO	K01915
OMA	ACFMPKP
OrthoDB	EOG6B360N
PhylomeDB	P0A9C5
BioCyc	EcoCyc:GLUTAMINESYN-MONOMER ECOL316407:JW3841-MONOMER MetaCyc:GLUTAMINESYN-MONOMER
SABIO-RK	P0A9C5
PRO	PR:P0A9C5
Proteomes	UP000000318 UP000000625
Genevestigator	P0A9C5
GO	GO:0005829 GO:0016020 GO:0005524 GO:0004356 GO:0042802 GO:0019676 GO:0006542 GO:0009399 GO:0019740
Gene3D	3.10.20.70 3.30.590.10
InterPro	IPR008147 IPR014746 IPR008146 IPR027303 IPR004809 IPR001637 IPR027302
Pfam	PF00120 PF03951
SUPFAM	SSF54368
TIGRFAMs	TIGR00653
PROSITE	PS00180 PS00182 PS00181

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0016020	membrane	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16858726^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019740	nitrogen utilization	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10383 PANTHER:PTN000464923	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10383 PANTHER:PTN000464923	C		Seeded From UniProt	complete
involved_in	GO:0006542	glutamine biosynthetic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000464923 UniProtKB:P9WN39	P		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10383 PANTHER:PTN000464923 UniProtKB:P15106 UniProtKB:P9WN39	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A9C5	F	occurs_in:(GO:0005737)	Seeded From UniProt	complete
involved_in	GO:0019740	nitrogen utilization	PMID:6102984^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019676	ammonia assimilation cycle	PMID:6102984^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	PMID:6102984^[3]	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:0004356	glutamate-ammonia ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004809 InterPro:IPR008146 InterPro:IPR008147 InterPro:IPR036651	F		Seeded From UniProt	complete
involved_in	GO:0006542	glutamine biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008147 InterPro:IPR036651	P		Seeded From UniProt	complete
involved_in	GO:0006807	nitrogen compound metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008146 InterPro:IPR008147 InterPro:IPR036651	P		Seeded From UniProt	complete
enables	GO:0004356	glutamate-ammonia ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.3.1.2	F		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:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		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
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
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Streicher, SL & Tyler, B (1980) Purification of glutamine synthetase from a variety of bacteria. J. Bacteriol. 142 69-78 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:16858726-1] 1.0 ^1.1 ^1.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 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:6102984-3] 3.0 ^3.1 ^3.2 Streicher, SL & Tyler, B (1980) Purification of glutamine synthetase from a variety of bacteria. J. Bacteriol. 142 69-78 PubMed GONUTS page

[PMID:27718375-4] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:18304323-5] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-6] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:GLNA

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