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ECOLI:GLNE

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) glnE
Protein Name(s) Glutamate-ammonia-ligase adenylyltransferase

Glutamine-synthetase adenylyltransferase ATase [Glutamate--ammonia-ligase] adenylyltransferase

External Links
UniProt P30870
EMBL Z21844
U00096
AP009048
PIR C65093
RefSeq NP_417525.1
YP_491245.1
PDB 1V4A
3K7D
PDBsum 1V4A
3K7D
ProteinModelPortal P30870
SMR P30870
DIP DIP-9780N
IntAct P30870
STRING 511145.b3053
PhosSite P0809395
PaxDb P30870
PRIDE P30870
EnsemblBacteria AAC76089
BAE77104
GeneID 12932521
947552
KEGG ecj:Y75_p2979
eco:b3053
PATRIC 32121518
EchoBASE EB1559
EcoGene EG11602
eggNOG COG1391
HOGENOM HOG000256491
InParanoid P30870
KO K00982
OMA ELRWLAR
OrthoDB EOG651SRZ
PhylomeDB P30870
BioCyc EcoCyc:GLNE-MONOMER
ECOL316407:JW3025-MONOMER
MetaCyc:GLNE-MONOMER
EvolutionaryTrace P30870
PRO PR:P30870
Proteomes UP000000318
UP000000625
Genevestigator P30870
GO GO:0008882
GO:0005524
HAMAP MF_00802
InterPro IPR023057
IPR005190
IPR013546
Pfam PF08335
PF03710

Annotations

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

involved_in

GO:0000820

regulation of glutamine family amino acid metabolic process

PMID:8412694[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:9312015[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:4920894[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:4934180[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

PMID:4920894[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11602
PANTHER:PTN000771322
UniProtKB:P9WN27

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11602
PANTHER:PTN000771322

C

Seeded From UniProt

complete

involved_in

GO:0000820

regulation of glutamine family amino acid metabolic process

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11602
PANTHER:PTN000771322
UniProtKB:P9WN27

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:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005190
InterPro:IPR023057

F

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013546

F

Seeded From UniProt

complete

enables

GO:0047388

[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.89

F

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.7.42

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

F

Seeded From UniProt

complete

enables

GO:0008882

[glutamate-ammonia-ligase] adenylyltransferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

F

Seeded From UniProt

complete

involved_in

GO:0000820

regulation of glutamine family amino acid metabolic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100229

P

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:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

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

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

enables

GO:0016779

nucleotidyltransferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0548

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

Notes

References

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

  1. van Heeswijk, WC et al. (1993) The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9 443-57 PubMed GONUTS page
  2. Jaggi, R et al. (1997) The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16 5562-71 PubMed GONUTS page
  3. 3.0 3.1 Ebner, E et al. (1970) ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. Eur. J. Biochem. 14 535-44 PubMed GONUTS page
  4. Anderson, WB & Stadtman, ER (1971) Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system. Arch. Biochem. Biophys. 143 428-43 PubMed GONUTS page
  5. 5.0 5.1 5.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page